|
Name |
Accession |
Description |
Interval |
E-value |
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
30-635 |
0e+00 |
|
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves repeated cycles of substrate binding and release. Hsp70 activity is ATP dependent. Hsp70 proteins are made up of two regions: the amino terminus is the ATPase domain and the carboxyl terminus is the substrate binding region.
Pssm-ID: 394970 [Multi-domain] Cd Length: 598 Bit Score: 981.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 30 VVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEgERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQ 109
Cdd:pfam00012 1 VIGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAFTPK-ERLVGQAAKNQAVTNPKNTVFSVKRLIGRKFSDPVVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 110 QDIKFLPFKVVEK-KTKPYIQVDIGGgqtKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAG 188
Cdd:pfam00012 80 RDIKHLPYKVVKLpNGDAGVEVRYLG---ETFTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 189 TIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIK 268
Cdd:pfam00012 157 QIAGLNVLRIVNEPTAAALAYGLDKTDKERNIAVYDLGGGTFDVSILEIGRGVFEVKATNGDTHLGGEDFDLRLVDHLAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 269 LYKKKTGKDVRKDNRAVQKLRREVEKAKRALSS-QHQARIEIESFYE-GEDFSETLTRAKFEELNMDLFRSTMKPVQKVL 346
Cdd:pfam00012 237 EFKKKYGIDLSKDKRALQRLREAAEKAKIELSSnQTNINLPFITAMAdGKDVSGTLTRAKFEELVADLFERTLEPVEKAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 347 EDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTGDLVLLDVCPLTLGI 426
Cdd:pfam00012 317 KDAGLSKSEIDEVVLVGGSTRIPAVQELVKEFF-GKEPSKGVNPDEAVAIGAAVQAGVLSGTFDVKDFLLLDVTPLSLGI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 427 ETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDVN 506
Cdd:pfam00012 396 ETLGGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDIDAN 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 507 GILRVTAEDKGTGNKNKITITNDQNrLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDKeklGGKL 586
Cdd:pfam00012 476 GILTVSAKDKGTGKEQEITIEASEG-LSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEE---GDKV 551
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1953100093 587 SSEDKEtmekAVEEKIEWLESH-QDADIEDFKAKKKELEEIVQPIISKLY 635
Cdd:pfam00012 552 PEAEKS----KVESAIEWLKDElEGDDKEEIEAKTEELAQVSQKIGERMY 597
|
|
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
31-639 |
0e+00 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 962.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 31 VGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTpEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQ 110
Cdd:PTZ00009 7 IGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVARNPENTVFDAKRLIGRKFDDSVVQS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 111 DIKFLPFKVVEK-KTKPYIQVDIGGgQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGT 189
Cdd:PTZ00009 86 DMKHWPFKVTTGgDDKPMIEVTYQG-EKKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATKDAGT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 190 IAGLNVMRIINEPTAAAIAYGLDKR-EGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIK 268
Cdd:PTZ00009 165 IAGLNVLRIINEPTAAAIAYGLDKKgDGEKNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVEFCVQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 269 LYKKKT-GKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLE 347
Cdd:PTZ00009 245 DFKRKNrGKDLSSNQRALRRLRTQCERAKRTLSSSTQATIEIDSLFEGIDYNVTISRARFEELCGDYFRNTLQPVEKVLK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 348 DSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGDQD--TGDLVLLDVCPLTLG 425
Cdd:PTZ00009 325 DAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFNGKEPCKSINPDEAVAYGAAVQAAILTGEQSsqVQDLLLLDVTPLSLG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 426 IETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDV 505
Cdd:PTZ00009 405 LETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEVTFDIDA 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 506 NGILRVTAEDKGTGNKNKITITNDQNRLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDkEKLGGK 585
Cdd:PTZ00009 485 NGILNVSAEDKSTGKSNKITITNDKGRLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQD-EKVKGK 563
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1953100093 586 LSSEDKETMEKAVEEKIEWLESHQDADIEDFKAKKKELEEIVQPIISKLYGSAG 639
Cdd:PTZ00009 564 LSDSDKATIEKAIDEALEWLEKNQLAEKEEFEHKQKEVESVCNPIMTKMYQAAG 617
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
28-653 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 917.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 28 GTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTwnDPS 107
Cdd:PRK00290 2 GKIIGIDLGTTNSCVAVMEGGEPKVIENAEGARTTPSVVAFTKDGERLVGQPAKRQAVTNPENTIFSIKRLMGRR--DEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 108 VQQDIKFLPFKVVEKKTKPYIqVDIGGgqtKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDA 187
Cdd:PRK00290 80 VQKDIKLVPYKIVKADNGDAW-VEIDG---KKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQATKDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 188 GTIAGLNVMRIINEPTAAAIAYGLDKrEGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFI 267
Cdd:PRK00290 156 GKIAGLEVLRIINEPTAAALAYGLDK-KGDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 268 KLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIE---IESFYEG-EDFSETLTRAKFEELNMDLFRSTMKPVQ 343
Cdd:PRK00290 235 DEFKKENGIDLRKDKMALQRLKEAAEKAKIELSSAQQTEINlpfITADASGpKHLEIKLTRAKFEELTEDLVERTIEPCK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 344 KVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVLSGDqdTGDLVLLDVCPLT 423
Cdd:PRK00290 315 QALKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVLAGD--VKDVLLLDVTPLS 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 424 LGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEI 503
Cdd:PRK00290 392 LGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVPQIEVTFDI 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 504 DVNGILRVTAEDKGTGNKNKITITNDQNrLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDkekLG 583
Cdd:PRK00290 472 DANGIVHVSAKDKGTGKEQSITITASSG-LSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKTLKE---LG 547
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953100093 584 GKLSSEDKETMEKAVEEkiewLES-HQDADIEDFKAKKKELEEIVQPIISKLYGSAGPPPTGDEEPADKDE 653
Cdd:PRK00290 548 DKVPADEKEKIEAAIKE----LKEaLKGEDKEAIKAKTEELTQASQKLGEAMYQQAQAAQGAAGAAAKDDD 614
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
28-405 |
0e+00 |
|
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; This subfamily includes human BiP (also known as HSP70 family protein 5 /HSPA5; 70-kDa heat shock protein 5; glucose-regulated protein 78/GRP78; immunoglobulin heavy chain-binding protein), Sacchaormyces cerevisiae BiP (also known as Grp78p), Arabidopsis thaliana BiP1-3 (also known as luminal-binding protein 1-3) and related proteins. BiP plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. It plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). BiP may function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. It appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating. BiP may also play a role in apoptosis and cell proliferation. Plant BiP may be required for pollen development and pollen tube growth. This subfamily belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466837 [Multi-domain] Cd Length: 376 Bit Score: 869.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 28 GTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTpEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPS 107
Cdd:cd10241 1 GTVIGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFT-DGERLIGDAAKNQATSNPENTVFDVKRLIGRKFDDKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 108 VQQDIKFLPFKVVEKKTKPYIQVDIGGgQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDA 187
Cdd:cd10241 80 VQKDIKLLPFKIVNKNGKPYIQVEVKG-EKKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 188 GTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFI 267
Cdd:cd10241 159 GTIAGLNVLRIINEPTAAAIAYGLDKKGGEKNILVFDLGGGTFDVSLLTIDNGVFEVLATNGDTHLGGEDFDQRVMDHFI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 268 KLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLE 347
Cdd:cd10241 239 KLFKKKTGKDISKDKRAVQKLRREVEKAKRALSSQHQARIEIESLFDGEDFSETLTRAKFEELNMDLFRKTLKPVQKVLE 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1953100093 348 DSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVL 405
Cdd:cd10241 319 DAGLKKSDIDEIVLVGGSTRIPKVQQLLKDFFNGKEPSRGINPDEAVAYGAAVQAGIL 376
|
|
| prok_dnaK |
TIGR02350 |
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ... |
30-635 |
0e+00 |
|
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE chaperone system. All members of the seed alignment were taken from completely sequenced bacterial or archaeal genomes and (except for Mycoplasma sequence) found clustered with other genes of this systems. This model excludes DnaK homologs that are not DnaK itself, such as the heat shock cognate protein HscA (TIGR01991). However, it is not designed to distinguish among DnaK paralogs in eukaryotes. Note that a number of dnaK genes have shadow ORFs in the same reverse (relative to dnaK) reading frame, a few of which have been assigned glutamate dehydrogenase activity. The significance of this observation is unclear; lengths of such shadow ORFs are highly variable as if the presumptive protein product is not conserved. [Protein fate, Protein folding and stabilization]
Pssm-ID: 274091 [Multi-domain] Cd Length: 595 Bit Score: 835.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 30 VVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDpsVQ 109
Cdd:TIGR02350 2 IIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFTKNGERLVGQPAKRQAVTNPENTIYSIKRFMGRRFDE--VT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 110 QDIKFLPFKVVEKKTKPYIQVDigggqTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGT 189
Cdd:TIGR02350 80 EEAKRVPYKVVGDGGDVRVKVD-----GKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 190 IAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKL 269
Cdd:TIGR02350 155 IAGLEVLRIINEPTAAALAYGLDKSKKDEKILVFDLGGGTFDVSILEIGDGVFEVLSTAGDTHLGGDDFDQRIIDWLADE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 270 YKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGED----FSETLTRAKFEELNMDLFRSTMKPVQKV 345
Cdd:TIGR02350 235 FKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLSTEINLPFITADASgpkhLEMTLTRAKFEELTADLVERTKEPVRQA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 346 LEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVLSGdqDTGDLVLLDVCPLTLG 425
Cdd:TIGR02350 315 LKDAGLSASDIDEVILVGGSTRIPAVQELVKDFF-GKEPNKSVNPDEVVAIGAAIQGGVLKG--DVKDVLLLDVTPLSLG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 426 IETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDV 505
Cdd:TIGR02350 392 IETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTFDIDA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 506 NGILRVTAEDKGTGNKNKITITNDQNrLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDkekLGGK 585
Cdd:TIGR02350 472 NGILHVSAKDKGTGKEQSITITASSG-LSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKE---AGDK 547
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1953100093 586 LSSEDKETMEKAVEEKIEWLEshqDADIEDFKAKKKELEEIVQPIISKLY 635
Cdd:TIGR02350 548 LPAEEKEKIEKAVAELKEALK---GEDVEEIKAKTEELQQALQKLAEAMY 594
|
|
| ASKHA_NBD_HSP70_HSPA1 |
cd10233 |
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ... |
31-405 |
0e+00 |
|
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; This subfamily includes human HSPA1A (70-kDa heat shock protein 1A, also known as HSP72; HSPA1; HSP70I; HSPA1B; HSP70-1; HSP70-1A), HSPA1B (70-kDa heat shock protein 1B, also known as HSPA1A; HSP70-2; HSP70-1B), and HSPA1L (70-kDa heat shock protein 1-like, also known as HSP70T; hum70t; HSP70-1L; HSP70-HOM), HSPA2 (70-kDa heat shock protein 2, also known as HSP70-2; HSP70-3), HSPA6 (also known as heat shock 70kDa protein 6; HSP70B'), HSPA7 (heat shock 70kDa protein 7 , also known as HSP70B), and HSPA8 (heat shock 70kDa protein 8, also known as Lipopolysaccharide-associated protein 1/LAP1; HSC70; HSP73; HSPA10). They are molecular chaperones implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. They play pivotal roles in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The subfamily also includes Saccharomyces cerevisiae heat shock protein Ssa1-4, which may play a role in the transport of polypeptides both across the mitochondrial membranes and into the endoplasmic reticulum. This subfamily belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466831 [Multi-domain] Cd Length: 375 Bit Score: 725.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 31 VGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTpEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQ 110
Cdd:cd10233 2 IGIDLGTTYSCVGVWQNDKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFDDPVVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 111 DIKFLPFKVVEKKTKPYIQVDIGGgQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTI 190
Cdd:cd10233 81 DMKHWPFKVVSGGDKPKIQVEYKG-ETKTFTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 191 AGLNVMRIINEPTAAAIAYGLDKR-EGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKL 269
Cdd:cd10233 160 AGLNVLRIINEPTAAAIAYGLDKKgKGERNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 270 YKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDS 349
Cdd:cd10233 240 FKRKHKKDISGNPRALRRLRTACERAKRTLSSSTQASIEIDSLFEGIDFYTSITRARFEELCADLFRSTLEPVEKVLRDA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1953100093 350 DLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVL 405
Cdd:cd10233 320 KLDKSQIHEIVLVGGSTRIPKVQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 375
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
28-653 |
0e+00 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 718.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 28 GTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPS 107
Cdd:PTZ00400 41 GDIVGIDLGTTNSCVAIMEGSQPKVIENSEGMRTTPSVVAFTEDGQRLVGIVAKRQAVTNPENTVFATKRLIGRRYDEDA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 108 VQQDIKFLPFKVVEKKT-KPYIQvdiggGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKD 186
Cdd:PTZ00400 121 TKKEQKILPYKIVRASNgDAWIE-----AQGKKYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQATKD 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 187 AGTIAGLNVMRIINEPTAAAIAYGLDKREGeKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHF 266
Cdd:PTZ00400 196 AGKIAGLDVLRIINEPTAAALAFGMDKNDG-KTIAVYDLGGGTFDISILEILGGVFEVKATNGNTSLGGEDFDQRILNYL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 267 IKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIE---IESFYEG-EDFSETLTRAKFEELNMDLFRSTMKPV 342
Cdd:PTZ00400 275 IAEFKKQQGIDLKKDKLALQRLREAAETAKIELSSKTQTEINlpfITADQSGpKHLQIKLSRAKLEELTHDLLKKTIEPC 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 343 QKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVLSGDqdTGDLVLLDVCPL 422
Cdd:PTZ00400 355 EKCIKDAGVKKDELNDVILVGGMTRMPKVSETVKKIF-GKEPSKGVNPDEAVAMGAAIQAGVLKGE--IKDLLLLDVTPL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 423 TLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFE 502
Cdd:PTZ00400 432 SLGIETLGGVFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPRGVPQIEVTFD 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 503 IDVNGILRVTAEDKGTGNKNKITITNDQNrLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDkekL 582
Cdd:PTZ00400 512 VDANGIMNISAVDKSTGKKQEITIQSSGG-LSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSVEKQLSD---L 587
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953100093 583 GGKLSSEDKETMekavEEKIEWLESH-QDADIEDFKAKKKELEEIVQPIISKLYGSAGPPPTGDEEPADKDE 653
Cdd:PTZ00400 588 KDKISDADKDEL----KQKITKLRSTlSSEDVDSIKDKTKQLQEASWKISQQAYKQGNSDNQQSEQSTNSEE 655
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
28-652 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 715.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 28 GTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDps 107
Cdd:PRK13411 2 GKVIGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFGKSGDRLVGQLAKRQAVTNAENTVYSIKRFIGRRWDD-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 108 VQQDIKFLPFKVVEKKTKPyIQVDIGGgqtKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDA 187
Cdd:PRK13411 80 TEEERSRVPYTCVKGRDDT-VNVQIRG---RNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 188 GTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFI 267
Cdd:PRK13411 156 GTIAGLEVLRIINEPTAAALAYGLDKQDQEQLILVFDLGGGTFDVSILQLGDGVFEVKATAGNNHLGGDDFDNCIVDWLV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 268 KLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIE---IESFYEGEDFSET-LTRAKFEELNMDLFRSTMKPVQ 343
Cdd:PRK13411 236 ENFQQQEGIDLSQDKMALQRLREAAEKAKIELSSMLTTSINlpfITADETGPKHLEMeLTRAKFEELTKDLVEATIEPMQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 344 KVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGDQDtgDLVLLDVCPLT 423
Cdd:PRK13411 316 QALKDAGLKPEDIDRVILVGGSTRIPAVQEAIQKFFGGKQPDRSVNPDEAVALGAAIQAGVLGGEVK--DLLLLDVTPLS 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 424 LGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEI 503
Cdd:PRK13411 394 LGIETLGEVFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRGVPQIEVSFEI 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 504 DVNGILRVTAEDKGTGNKNKITITNdQNRLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDKEKLg 583
Cdd:PRK13411 474 DVNGILKVSAQDQGTGREQSIRITN-TGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSYESTLKENGEL- 551
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953100093 584 gkLSSEDKETMEKAVEEkIEWLESHQDADIEDFKAKKKELEEIVQPIISKLYGSAGPPPTGDEEPADKD 652
Cdd:PRK13411 552 --ISEELKQRAEQKVEQ-LEAALTDPNISLEELKQQLEEFQQALLAIGAEVYQQGGSQTTDTVEPTSDT 617
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
30-542 |
0e+00 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 713.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 30 VVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDpsvq 109
Cdd:COG0443 1 AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFPKDGEVLVGEAAKRQAVTNPGRTIRSIKRLLGRSLFD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 110 qdikflpfkvvekktkpyIQVDIGGgqtKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGT 189
Cdd:COG0443 77 ------------------EATEVGG---KRYSPEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAAR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 190 IAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKL 269
Cdd:COG0443 136 IAGLEVLRLLNEPTAAALAYGLDKGKEEETILVYDLGGGTFDVSILRLGDGVFEVLATGGDTHLGGDDFDQALADYVAPE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 270 YKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIeSFYEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDS 349
Cdd:COG0443 216 FGKEEGIDLRLDPAALQRLREAAEKAKIELSSADEAEINL-PFSGGKHLDVELTRAEFEELIAPLVERTLDPVRQALADA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 350 DLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTgdlvlLDVCPLTLGIETV 429
Cdd:COG0443 295 GLSPSDIDAVLLVGGSTRMPAVRERVKELF-GKEPLKGVDPDEAVALGAAIQAGVLAGDVKD-----LDVTPLSLGIETL 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 430 GGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDVNGIL 509
Cdd:COG0443 369 GGVFTKLIPRNTTIPTAKSQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDANGIL 448
|
490 500 510
....*....|....*....|....*....|...
gi 1953100093 510 RVTAEDKGTGNKNKITITndqnrltpEEIERMV 542
Cdd:COG0443 449 SVSAKDLGTGKEQSITIK--------EEIERML 473
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
28-652 |
0e+00 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 708.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 28 GTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDps 107
Cdd:CHL00094 2 GKVVGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYTKKGDLLVGQIAKRQAVINPENTFYSVKRFIGRKFSE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 108 VQQDIKFLPFKVVeKKTKPYIQVDIGGGQtKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDA 187
Cdd:CHL00094 80 ISEEAKQVSYKVK-TDSNGNIKIECPALN-KDFSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATKDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 188 GTIAGLNVMRIINEPTAAAIAYGLDKREGEKnILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFI 267
Cdd:CHL00094 158 GKIAGLEVLRIINEPTAASLAYGLDKKNNET-ILVFDLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDKKIVNWLI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 268 KLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIE---IESFYEG-EDFSETLTRAKFEELNMDLFRSTMKPVQ 343
Cdd:CHL00094 237 KEFKKKEGIDLSKDRQALQRLTEAAEKAKIELSNLTQTEINlpfITATQTGpKHIEKTLTRAKFEELCSDLINRCRIPVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 344 KVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVLSGDqdTGDLVLLDVCPLT 423
Cdd:CHL00094 317 NALKDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLL-GKKPNQSVNPDEVVAIGAAVQAGVLAGE--VKDILLLDVTPLS 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 424 LGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEI 503
Cdd:CHL00094 394 LGVETLGGVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQIEVTFDI 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 504 DVNGILRVTAEDKGTGNKNKITITNDQNrLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIgdkEKLG 583
Cdd:CHL00094 474 DANGILSVTAKDKGTGKEQSITIQGAST-LPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQL---KELK 549
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953100093 584 GKLSSEDKETMEKAVEEKIEWLEShqdADIEDFKAKKKELEEIVQPIISKLY--GSAGPPPTGDEEPADKD 652
Cdd:CHL00094 550 DKISEEKKEKIENLIKKLRQALQN---DNYESIKSLLEELQKALMEIGKEVYssTSTTDPASNDDDVIDTD 617
|
|
| ASKHA_NBD_HSP70_HSPA1-like |
cd24028 |
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ... |
30-405 |
0e+00 |
|
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The HSPA1-like family includes human HSPA1A (70-kDa heat shock protein 1A, also known as HSP72; HSPA1; HSP70I; HSPA1B; HSP70-1; HSP70-1A), HSPA1B (70-kDa heat shock protein 1B, also known as HSPA1A; HSP70-2; HSP70-1B), and HSPA1L (70-kDa heat shock protein 1-like, also known as HSP70T; hum70t; HSP70-1L; HSP70-HOM), HSPA2 (70-kDa heat shock protein 2, also known as HSP70-2; HSP70-3), BiP (also known as HSP70 family protein 5 /HSPA5; 70-kDa heat shock protein 5; glucose-regulated protein 78/GRP78; immunoglobulin heavy chain-binding protein), HSPA6 (also known as heat shock 70kDa protein 6; HSP70B'), HSPA7 (heat shock 70kDa protein 7 , also known as HSP70B), HSPA8 (heat shock 70kDa protein 8, also known as Lipopolysaccharide-associated protein 1/LAP1; HSC70; HSP73; HSPA10), HSPA13 (also known as 70-kDa heat shock protein 13; STCH; microsomal stress-70 protein ATPase core; stress-70 protein chaperone microsome-associated 60 kDa protein), as well as Saccharmoyces cerevisiae Hsp70 chaperone Ssb1-2 and heat shock protein Ssa1-4. HSPA1A/1B, HSPA1L, HSPA2 and HSPA6-8 are molecular chaperones implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. They play pivotal roles in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. BiP plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. It plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). HSPA13 has peptide-independent ATPase activity. All family members belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466878 [Multi-domain] Cd Length: 376 Bit Score: 692.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 30 VVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTpEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQ 109
Cdd:cd24028 1 AIGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSYVAFT-DGERLVGEAAKNQAASNPENTIFDVKRLIGRKFDDPSVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 110 QDIKFLPFKVVEKKT-KPYIQVDIGGgQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAG 188
Cdd:cd24028 80 SDIKHWPFKVVEDEDgKPKIEVTYKG-EEKTFSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 189 TIAGLNVMRIINEPTAAAIAYGLDKR-EGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFI 267
Cdd:cd24028 159 TIAGLNVLRIINEPTAAALAYGLDKKsSGERNVLVFDLGGGTFDVSLLSIDNGVFEVKATAGDTHLGGEDFDNRLVEYLV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 268 KLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLE 347
Cdd:cd24028 239 EEFKKKHGKDLRENPRAMRRLRSACERAKRTLSTSTSATIEIDSLYDGIDFETTITRAKFEELCEDLFKKCLEPVEKVLK 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1953100093 348 DSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVL 405
Cdd:cd24028 319 DAKLSKDDIDEVVLVGGSTRIPKIQELLSEFFGGKELCKSINPDEAVAYGAAIQAAIL 376
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
28-614 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 678.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 28 GTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDps 107
Cdd:PRK13410 2 GRIVGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFTKDGELLVGQLARRQLVLNPQNTFYNLKRFIGRRYDE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 108 VQQDIKFLPFKVvekKTKPYIQVDIGGGQT-KTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKD 186
Cdd:PRK13410 80 LDPESKRVPYTI---RRNEQGNVRIKCPRLeREFAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATRD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 187 AGTIAGLNVMRIINEPTAAAIAYGLDKREgEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHF 266
Cdd:PRK13410 157 AGRIAGLEVERILNEPTAAALAYGLDRSS-SQTVLVFDLGGGTFDVSLLEVGNGVFEVKATSGDTQLGGNDFDKRIVDWL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 267 IKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGED----FSETLTRAKFEELNMDLFRSTMKPV 342
Cdd:PRK13410 236 AEQFLEKEGIDLRRDRQALQRLTEAAEKAKIELSGVSVTDISLPFITATEDgpkhIETRLDRKQFESLCGDLLDRLLRPV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 343 QKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVLSGDqdTGDLVLLDVCPL 422
Cdd:PRK13410 316 KRALKDAGLSPEDIDEVVLVGGSTRMPMVQQLVRTLI-PREPNQNVNPDEVVAVGAAIQAGILAGE--LKDLLLLDVTPL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 423 TLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFE 502
Cdd:PRK13410 393 SLGLETIGGVMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQVAFD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 503 IDVNGILRVTAEDKGTGNKNKITITNDQNrLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDKE-K 581
Cdd:PRK13410 473 IDANGILQVSATDRTTGREQSVTIQGAST-LSEQEVNRMIQEAEAKADEDRRRRERIEKRNRALTLIAQAERRLRDAAlE 551
|
570 580 590
....*....|....*....|....*....|...
gi 1953100093 582 LGGKLSSEDKETMEKAVEEKIEWLESHQDADIE 614
Cdd:PRK13410 552 FGPYFAERQRRAVESAMRDVQDSLEQDDDRELD 584
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
30-650 |
0e+00 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 658.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 30 VVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDpsVQ 109
Cdd:PLN03184 41 VVGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTKNGDRLVGQIAKRQAVVNPENTFFSVKRFIGRKMSE--VD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 110 QDIKFLPFKVVeKKTKPYIQVD---IGggqtKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKD 186
Cdd:PLN03184 119 EESKQVSYRVV-RDENGNVKLDcpaIG----KQFAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKD 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 187 AGTIAGLNVMRIINEPTAAAIAYGLDKREGEkNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHF 266
Cdd:PLN03184 194 AGRIAGLEVLRIINEPTAASLAYGFEKKSNE-TILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRIVDWL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 267 IKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIE---IESFYEGEDFSET-LTRAKFEELNMDLFRSTMKPV 342
Cdd:PLN03184 273 ASNFKKDEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTSISlpfITATADGPKHIDTtLTRAKFEELCSDLLDRCKTPV 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 343 QKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFfNGKEPSRGINPDEAVAYGAAVQAGVLSGDqdTGDLVLLDVCPL 422
Cdd:PLN03184 353 ENALRDAKLSFKDIDEVILVGGSTRIPAVQELVKKL-TGKDPNVTVNPDEVVALGAAVQAGVLAGE--VSDIVLLDVTPL 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 423 TLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFE 502
Cdd:PLN03184 430 SLGLETLGGVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVKFD 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 503 IDVNGILRVTAEDKGTGNKNKITITNdQNRLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIgdkEKL 582
Cdd:PLN03184 510 IDANGILSVSATDKGTGKKQDITITG-ASTLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTEKQL---KEL 585
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953100093 583 GGKLSSEDKETMEKAVEEKIEWLEShqdADIEDFKAKKKELEEIVQPIISKLYGSAGPPPTGDEEPAD 650
Cdd:PLN03184 586 GDKVPADVKEKVEAKLKELKDAIAS---GSTQKMKDAMAALNQEVMQIGQSLYNQPGAGGAGPAPGGE 650
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
28-627 |
0e+00 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 622.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 28 GTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEgERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPS 107
Cdd:PTZ00186 27 GDVIGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAFKGS-EKLVGLAAKRQAITNPQSTFYAVKRLIGRRFEDEH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 108 VQQDIKFLPFKVVEKKT-KPYIQvdigGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKD 186
Cdd:PTZ00186 106 IQKDIKNVPYKIVRAGNgDAWVQ----DGNGKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQATKD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 187 AGTIAGLNVMRIINEPTAAAIAYGLDKREgEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHF 266
Cdd:PTZ00186 182 AGTIAGLNVIRVVNEPTAAALAYGMDKTK-DSLIAVYDLGGGTFDISVLEIAGGVFEVKATNGDTHLGGEDFDLALSDYI 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 267 IKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGEDFSE----TLTRAKFEELNMDLFRSTMKPV 342
Cdd:PTZ00186 261 LEEFRKTSGIDLSKERMALQRVREAAEKAKCELSSAMETEVNLPFITANADGAQhiqmHISRSKFEGITQRLIERSIAPC 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 343 QKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVLSGDqdTGDLVLLDVCPL 422
Cdd:PTZ00186 341 KQCMKDAGVELKEINDVVLVGGMTRMPKVVEEVKKFF-QKDPFRGVNPDEAVALGAATLGGVLRGD--VKGLVLLDVTPL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 423 TLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFE 502
Cdd:PTZ00186 418 SLGIETLGGVFTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQIEVTFD 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 503 IDVNGILRVTAEDKGTGNKNKITITNDQNrLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDKEkl 582
Cdd:PTZ00186 498 IDANGICHVTAKDKATGKTQNITITANGG-LSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAETQLTTAERQLGEWK-- 574
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1953100093 583 ggKLSSEDKETMEKAVEEKIEWLESHQDADiEDFKAKKKELEEIV 627
Cdd:PTZ00186 575 --YVSDAEKENVKTLVAELRKAMENPNVAK-DDLAAATDKLQKAV 616
|
|
| ASKHA_NBD_HSP70_DnaK-like |
cd10234 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ... |
30-406 |
0e+00 |
|
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar proteins; This subfamily includes Escherichia coli chaperone protein DnaK (also known as heat shock 70 kDa protein/HSP70), human mitochondrial heat shock 70 kDa protein HSPA9 (also known as mitochondrial stress-70 protein; mortalin; 75 kDa glucose-regulated protein/GRP-75; HSPA9B; MOT; peptide-binding protein 74/PBP74), Saccharomyces cerevisiae stress-seventy subfamily C proteins, Ssc1p (also called import motor subunit, mitochondrial; endonuclease SceI 75 kDa subunit; mtHSP70; ENS1; endonuclease SceI 75 kDa subunit) and Ssc3p (also called extracellular mutant protein 10/Ecm10), and Saccharomyces cerevisiae Stress-seventy subfamily Q protein 1/Ssq1p (also called Ssc2p; Ssh1p; mtHSP70 homolog). They all belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs); for Escherichia coli DnaK, these are the DnaJ and GrpE, respectively.
Pssm-ID: 466832 [Multi-domain] Cd Length: 373 Bit Score: 566.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 30 VVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQ 109
Cdd:cd10234 1 IIGIDLGTTNSCVAVMEGGKPTVIPNAEGGRTTPSVVAFTKDGERLVGQPAKRQAVTNPENTIFSIKRFMGRRYKEVEVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 110 QDIKFLPfkvVEKKTKPYIQVDIGGgqtKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGT 189
Cdd:cd10234 81 RKQVPYP---VVSAGNGDAWVEIGG---KEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 190 IAGLNVMRIINEPTAAAIAYGLDKREGEKnILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKL 269
Cdd:cd10234 155 IAGLEVLRIINEPTAAALAYGLDKKKDEK-ILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 270 YKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIE---IESFYEG-EDFSETLTRAKFEELNMDLFRSTMKPVQKV 345
Cdd:cd10234 234 FKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLETEINlpfITADASGpKHLEMKLTRAKFEELTEDLVERTIEPVEQA 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953100093 346 LEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVLS 406
Cdd:cd10234 314 LKDAKLSPSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVLA 373
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
31-405 |
0e+00 |
|
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar proteins; Ssb is ribosome-bound, Hsp70-type chaperone that assists in the co-translational folding of newly synthesized proteins in the cytosol. It stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably until fully synthesized. Ssb cooperates with a specific Hsp40/Hsp70 co-chaperone termed the ribosome-associated complex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substrate binding state. Saccharmoyces cerevisiae Ssb are encoded by two genes, SSB1 and SSB2. Ssb1p is also known as cold-inducible protein YG101. Members in this subfamily belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466943 [Multi-domain] Cd Length: 375 Bit Score: 560.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 31 VGIDLGTTYSCVGVFKNGrVEIIANDQGNRITPSYVAFTPEgERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQ 110
Cdd:cd24093 2 IGIDLGTTYSCVATYESS-VEIIANEQGNRVTPSFVAFTPE-ERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 111 DIKFLPFKVVEKKTKPYIQVDIGGgQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTI 190
Cdd:cd24093 80 DMKTWPFKVIDVNGNPVIEVQYLG-ETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 191 AGLNVMRIINEPTAAAIAYGLD--KREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIK 268
Cdd:cd24093 159 AGLNVLRIINEPTAAAIAYGLGagKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 269 LYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLED 348
Cdd:cd24093 239 EFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSITRARFEDLNAALFKSTLEPVEQVLKD 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1953100093 349 SDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVL 405
Cdd:cd24093 319 AKISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLEKSINPDEAVAYGAAVQGAIL 375
|
|
| HscA |
TIGR01991 |
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ... |
30-633 |
0e+00 |
|
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act together as chaperones. HscA resembles DnaK but belongs in a separate clade. The apparent function is to aid assembly of iron-sulfur cluster proteins. Homologs from Buchnera and Wolbachia are clearly in the same clade but are highly derived and score lower than some examples of DnaK. [Protein fate, Protein folding and stabilization]
Pssm-ID: 273915 [Multi-domain] Cd Length: 599 Bit Score: 553.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 30 VVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPsvq 109
Cdd:TIGR01991 1 AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYLKDGGVEVGKEALAAAAEDPKNTISSVKRLMGRSIEDI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 110 QDIKFLPFKVVEKKTKpYIQVDIGGGqTKTfaPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGT 189
Cdd:TIGR01991 78 KTFSILPYRFVDGPGE-MVRLRTVQG-TVT--PVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQATKDAAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 190 IAGLNVMRIINEPTAAAIAYGLDKREgEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIkl 269
Cdd:TIGR01991 154 LAGLNVLRLLNEPTAAAVAYGLDKAS-EGIYAVYDLGGGTFDVSILKLTKGVFEVLATGGDSALGGDDFDHALAKWIL-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 270 ykKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIEsfYEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDS 349
Cdd:TIGR01991 231 --KQLGISADLNPEDQRLLLQAARAAKEALTDAESVEVDFT--LDGKDFKGKLTRDEFEALIQPLVQKTLSICRRALRDA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 350 DLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTGDLVLLDVCPLTLGIETV 429
Cdd:TIGR01991 307 GLSVEEIKGVVLVGGSTRMPLVRRAVAELF-GQEPLTDIDPDQVVALGAAIQADLLAGNRIGNDLLLLDVTPLSLGIETM 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 430 GGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDVNGIL 509
Cdd:TIGR01991 386 GGLVEKIIPRNTPIPVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFELRGIPPMVAGAARIRVTFQVDADGLL 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 510 RVTAEDKGTGNKNKITITNDQNrLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDKEKLggkLSSE 589
Cdd:TIGR01991 466 TVSAQEQSTGVEQSIQVKPSYG-LSDEEIERMLKDSFKHAEEDMYARALAEQKVEAERILEALQAALAADGDL---LSED 541
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1953100093 590 DKETMEKAVEEKIEWLeshQDADIEDFKAKKKELEEIVQPIISK 633
Cdd:TIGR01991 542 ERAAIDAAMEALQKAL---QGDDADAIKAAIEALEEATDNFAAR 582
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
31-614 |
0e+00 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 545.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 31 VGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGeRLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDpsVQQ 110
Cdd:PRK05183 22 VGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLEDG-IEVGYEARANAAQDPKNTISSVKRFMGRSLAD--IQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 111 DIKFLPFKVVEKK-TKPYIQVDIGggqTKTfaPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGT 189
Cdd:PRK05183 99 RYPHLPYQFVASEnGMPLIRTAQG---LKS--PVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQATKDAAR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 190 IAGLNVMRIINEPTAAAIAYGLDKREgEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKl 269
Cdd:PRK05183 174 LAGLNVLRLLNEPTAAAIAYGLDSGQ-EGVIAVYDLGGGTFDISILRLSKGVFEVLATGGDSALGGDDFDHLLADWILE- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 270 ykkKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIEsfyegeDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDS 349
Cdd:PRK05183 252 ---QAGLSPRLDPEDQRLLLDAARAAKEALSDADSVEVSVA------LWQGEITREQFNALIAPLVKRTLLACRRALRDA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 350 DLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTGDLVLLDVCPLTLGIETV 429
Cdd:PRK05183 323 GVEADEVKEVVMVGGSTRVPLVREAVGEFF-GRTPLTSIDPDKVVAIGAAIQADILAGNKPDSDMLLLDVIPLSLGLETM 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 430 GGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDVNGIL 509
Cdd:PRK05183 402 GGLVEKIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQVDADGLL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 510 RVTAEDKGTGNKNKITITNDQNrLTPEEIERMVNDAEKFAEEDKK---LKE-RIDTRNELESYAYSLKnqigdkeKLGGK 585
Cdd:PRK05183 482 SVTAMEKSTGVEASIQVKPSYG-LTDDEIARMLKDSMSHAEEDMQaraLAEqKVEAERVLEALQAALA-------ADGDL 553
|
570 580
....*....|....*....|....*....
gi 1953100093 586 LSSEDKETMEKAVEEKIEWLESHQDADIE 614
Cdd:PRK05183 554 LSAAERAAIDAAMAALREVAQGDDADAIE 582
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
28-405 |
0e+00 |
|
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and similar proteins; This subgroup includes human mitochondrial HSPA9 (also known as mitochondrial stress-70 protein; mortalin; 75 kDa glucose-regulated protein/GRP-75; HSPA9B; MOT; peptide-binding protein 74/PBP74). It acts as a chaperone protein which plays an important role in mitochondrial iron-sulfur cluster (ISC) biogenesis. It interacts with and stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU. HSPA9 regulates erythropoiesis via stabilization of ISC assembly. It may play a role in the control of cell proliferation and cellular aging. Members in this subgroup belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466839 [Multi-domain] Cd Length: 377 Bit Score: 520.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 28 GTVVGIDLGTTYSCVGVF--KNGRVeiIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWND 105
Cdd:cd11733 1 GDVIGIDLGTTNSCVAVMegKTPKV--IENAEGARTTPSVVAFTADGERLVGMPAKRQAVTNPENTLYATKRLIGRRFDD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 106 PSVQQDIKFLPFKVVeKKTKPYIQVDIGGgqtKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATK 185
Cdd:cd11733 79 PEVQKDIKMVPYKIV-KASNGDAWVEAHG---KKYSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQATK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 186 DAGTIAGLNVMRIINEPTAAAIAYGLDKREGeKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEH 265
Cdd:cd11733 155 DAGQIAGLNVLRIINEPTAAALAYGLDKKDD-KIIAVYDLGGGTFDISILEIQKGVFEVKATNGDTFLGGEDFDNALLNY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 266 FIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIEsfYEGEDFSE------TLTRAKFEELNMDLFRSTM 339
Cdd:cd11733 234 LVAEFKKEQGIDLSKDNLALQRLREAAEKAKIELSSSLQTDINLP--FITADASGpkhlnmKLTRAKFESLVGDLIKRTV 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953100093 340 KPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVL 405
Cdd:cd11733 312 EPCKKCLKDAGVSKSDIGEVLLVGGMTRMPKVQETVQEIF-GKAPSKGVNPDEAVAMGAAIQGGVL 376
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
28-407 |
2.29e-164 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein Ssc1p and Ssc3p and similar proteins; This subgroup includes Saccharomyces cerevisiae Stress-Seventy subfamily C proteins, Ssc1p (also called import motor subunit, mitochondrial; endonuclease SceI 75 kDa subunit; mtHSP70; ENS1; endonuclease SceI 75 kDa subunit) and sc3p (also called extracellular mutant protein 10/Ecm10). Ssc1p is an essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. It constitutes the ATP-driven core of the motor and binds the precursor preprotein. It is required for the import of the processed frataxin homolog YFH1 into the mitochondrion. Ssc1p also acts as a non-catalytic component of endonuclease SceI (endo.SceI), which cleaves specifically at multiple sites on mitochondrial DNA and produces double-stranded breaks. Ssc1p confers broader sequence specificity, greater stability, and higher activity on the catalytic subunit. Ssc3p plays a role in facilitating the assembly of some protein complexes inside the mitochondria. It may initiate the events that lead to refolding of imported precursors in the matrix space.
Pssm-ID: 466840 [Multi-domain] Cd Length: 378 Bit Score: 475.78 E-value: 2.29e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 28 GTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPS 107
Cdd:cd11734 1 GPVIGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVVAFTKDGERLVGVPAKRQAVVNPENTLFATKRLIGRKFDDAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 108 VQQDIKFLPFKVVeKKTKPYIQVDIGGgqtKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDA 187
Cdd:cd11734 81 VQRDIKEVPYKIV-KHSNGDAWVEARG---QKYSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATKDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 188 GTIAGLNVMRIINEPTAAAIAYGLDKrEGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFI 267
Cdd:cd11734 157 GQIAGLNVLRVINEPTAAALAYGLDK-SGDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTHLGGEDFDIALVRHIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 268 KLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGED----FSETLTRAKFEELNMDLFRSTMKPVQ 343
Cdd:cd11734 236 SEFKKESGIDLSKDRMAIQRIREAAEKAKIELSSTLQTDINLPFITADASgpkhINMKLTRAQFESLVKPLVDRTVEPCK 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953100093 344 KVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVLSG 407
Cdd:cd11734 316 KALKDAGVKTSEINEVILVGGMSRMPKVQETVKSIF-GREPSKGVNPDEAVAIGAAIQGGVLSG 378
|
|
| ASKHA_NBD_HSP70_HscA |
cd10236 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
30-407 |
6.81e-158 |
|
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar proteins; Escherichia coli HscA, also called Hsc66, acts as a chaperone involved in the maturation of iron-sulfur cluster-containing proteins. It has a low intrinsic ATPase activity which is markedly stimulated by HscB. It is involved in the maturation of IscU. Members in this subfamily belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). HscA's partner J-domain protein is HscB; it does not appear to require a NEF and has been shown to be induced by cold-shock. The HscA-HscB chaperone/co-chaperone pair is involved in [Fe-S] cluster assembly.
Pssm-ID: 466834 [Multi-domain] Cd Length: 367 Bit Score: 458.60 E-value: 6.81e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 30 VVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDpsVQ 109
Cdd:cd10236 4 AVGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVHYGEDGKITVGEKAKENAITDPENTISSVKRLMGRSLAD--VK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 110 QDIKFLPFKVVEKkTKPYIQVDIGGGqtkTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGT 189
Cdd:cd10236 82 EELPLLPYRLVGD-ENELPRFRTGAG---NLTPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 190 IAGLNVMRIINEPTAAAIAYGLDKrEGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIkl 269
Cdd:cd10236 158 LAGLNVLRLLNEPTAAALAYGLDQ-KKEGTIAVYDLGGGTFDISILRLSDGVFEVLATGGDTALGGDDFDHLLADWIL-- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 270 ykKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESfyEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDS 349
Cdd:cd10236 235 --KQIGIDARLDPAVQQALLQAARRAKEALSDADSASIEVEV--EGKDWEREITREEFEELIQPLVKRTLEPCRRALKDA 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1953100093 350 DLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVLSG 407
Cdd:cd10236 311 GLEPADIDEVVLVGGSTRIPLVRQRVAEFF-GREPLTSINPDEVVALGAAIQADILAG 367
|
|
| ASKHA_NBD_HSP70_HSPA13 |
cd10237 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
29-407 |
4.36e-155 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; HSPA13, also called 70-kDa heat shock protein 13, STCH, microsomal stress-70 protein ATPase core, or stress-70 protein chaperone microsome-associated 60 kDa protein, has peptide-independent ATPase activity. It belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). HSPA13 contains an NBD but lacks an SBD. It may function to regulate cell proliferation and survival and modulate the TRAIL-mediated cell death pathway. The HSPA13 gene is a candidate stomach cancer susceptibility gene; a mutation in the NBD coding region of HSPA13 has been identified in stomach cancer cells. The NBD of HSPA13 interacts with the ubiquitin-like proteins Chap1 and Chap2, implicating HSPA13 in regulating cell cycle and cell death events. HSPA13 is induced by the Ca2+ ionophore A23187.
Pssm-ID: 466835 [Multi-domain] Cd Length: 409 Bit Score: 453.33 E-value: 4.36e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 29 TVVGIDLGTTYSCVGVFK--NGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDP 106
Cdd:cd10237 23 KIVGIDLGTTYSCVGVYHavTGEVEVIPDDDGHKSIPSVVAFTPDGGVLVGYDALAQAEHNPSNTIYDAKRFIGKTFTKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 107 SVQQDIKFLPFKVVEK---KTKPYIQVDiggGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQA 183
Cdd:cd10237 103 ELEEEAKRYPFKVVNDnigSAFFEVPLN---GSTLVVSPEDIGSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRNA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 184 TKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVM 263
Cdd:cd10237 180 TRKAANLAGLEVLRVINEPTAAAMAYGLHKKSDVNNVLVVDLGGGTLDVSLLNVQGGMFLTRAMAGNNHLGGQDFNQRLF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 264 EHFIKLYKKKTGKDVrKDNRAVQKLRREVEKAKRALSSQHQARIEIE--SFYEGED---FSETLTRAKFEELNMDLFRST 338
Cdd:cd10237 260 QYLIDRIAKKFGKTL-TDKEDIQRLRQAVEEVKLNLTNHNSASLSLPlqISLPSAFkvkFKEEITRDLFETLNEDLFQRV 338
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953100093 339 MKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVLSG 407
Cdd:cd10237 339 LEPIRQVLAEVELGKEDVDEIVLVGGSTRIPRVRQLVREFF-GKDPNTSVDPELAVVTGVAIQAGIIGG 406
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
31-406 |
1.33e-149 |
|
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and similar proteins; Escherichia coli DnaK, also called heat shock 70 kDa protein/HSP70, plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Moreover, DnaK participates actively in the response to hyperosmotic shock. Escherichia coli HscA, also called Hsc66, acts as a chaperone involved in the maturation of iron-sulfur cluster-containing proteins. It has a low intrinsic ATPase activity which is markedly stimulated by HscB. It is involved in the maturation of IscU. Escherichia coli HscC, also called Hsc62, or YbeW, may act as the chaperone. It has ATPase activity. It cannot be stimulated by DnaJ. The family also includes Saccharomyces cerevisiae stress-seventy subfamily C proteins, Ssc1p (also called import motor subunit, mitochondrial; endonuclease SceI 75 kDa subunit; mtHSP70; ENS1; endonuclease SceI 75 kDa subunit) and Ssc3p (also called extracellular mutant protein 10/Ecm10), and Saccharomyces cerevisiae Stress-seventy subfamily Q protein 1/Ssq1p (also called Ssc2p; Ssh1p; mtHSP70 homolog). They all belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs); for Escherichia coli DnaK, these are the DnaJ and GrpE, respectively.
Pssm-ID: 466879 [Multi-domain] Cd Length: 351 Bit Score: 437.01 E-value: 1.33e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 31 VGIDLGTTYSCVGVFKNGRVEIIA-NDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSvq 109
Cdd:cd24029 1 VGIDLGTTNSAVAYWDGNGAEVIIeNSEGKRTTPSVVYFDKDGEVLVGEEAKNQALLDPENTIYSVKRLMGRDTKDKE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 110 qdikflpfkvvekktkpyiqvDIGGgqtKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGT 189
Cdd:cd24029 79 ---------------------EIGG---KEYTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 190 IAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKL 269
Cdd:cd24029 135 LAGLNVLRLINEPTAAALAYGLDKEGKDGTILVYDLGGGTFDVSILEIENGKFEVLATGGDNFLGGDDFDEAIAELILEK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 270 YKKKTGK-DVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLED 348
Cdd:cd24029 215 IGIETGIlDDKEDERARARLREAAEEAKIELSSSDSTDILILDDGKGGELEIEITREEFEELIAPLIERTIDLLEKALKD 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1953100093 349 SDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVLS 406
Cdd:cd24029 295 AKLSPEDIDRVLLVGGSSRIPLVREMLEEYF-GREPISSVDPDEAVAKGAAIYAASLA 351
|
|
| ASKHA_NBD_HSP70_HSPA14 |
cd10238 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ... |
29-405 |
1.92e-140 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; HSPA14, also called HSP70-like protein 1 (Hsp70L1), or heat shock protein HSP60, is a component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, HSPA14 binds to the nascent polypeptide chain, while DNAJC2 stimulates its ATPase activity. It belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis.
Pssm-ID: 466836 [Multi-domain] Cd Length: 377 Bit Score: 414.33 E-value: 1.92e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 29 TVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEgERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSV 108
Cdd:cd10238 1 AAFGVHFGNTNACVAVYKDGRTDVVANDAGDRVTPAVVAFTDN-EKIVGLAAKQGLIRNASNTVVRVKQLLGRSFDDPAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 109 QQDIKFLPFKVVEKKTKPYIQVDIGGgQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAG 188
Cdd:cd10238 80 QELKKESKCKIIEKDGKPGYEIELEE-KKKLVSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 189 TIAGLNVMRIINEPTAAAIAYGL--DKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHF 266
Cdd:cd10238 159 EKAGFNVLRVISEPSAAALAYGIgqDDPTENSNVLVYRLGGTSLDVTVLSVNNGMYRVLATRTDDNLGGDDFTEALAEHL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 267 IKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVL 346
Cdd:cd10238 239 ASEFKRQWKQDVRENKRAMAKLMNAAEVCKHVLSTLNTATCSVESLYDGMDFQCNVSRARFESLCSSLFQQCLEPIQEVL 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1953100093 347 EDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVL 405
Cdd:cd10238 319 NSAGLTKEDIDKVILCGGSSRIPKLQQLIKDLFPSAEVLSSIPPDEVIAIGAAKQAGLL 377
|
|
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
31-403 |
1.05e-135 |
|
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar proteins; Escherichia coli HscC, also called Hsc62, or YbeW, may act as the chaperone. It has ATPase activity. It cannot be stimulated by DnaJ. Members in this subfamily belong to the heat shock protein 70 (Hsp70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, Hsp70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Two genes in the vicinity of the HscC gene code for potential cochaperones: J-domain containing proteins, DjlB/YbeS and DjlC/YbeV. HscC and its co-chaperone partners may play a role in the SOS DNA damage response. HscC does not appear to require a NEF.
Pssm-ID: 466833 [Multi-domain] Cd Length: 343 Bit Score: 401.24 E-value: 1.05e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 31 VGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGrtwndpsvqq 110
Cdd:cd10235 1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVVSVDEDGSILVGRAAKERLVTHPDRTAASFKRFMG---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 111 dikflpfkvvekKTKPYIqvdIGGgqtKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTI 190
Cdd:cd10235 71 ------------TDKQYR---LGN---HTFRAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGEL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 191 AGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLY 270
Cdd:cd10235 133 AGLKVERLINEPTAAALAYGLHKREDETRFLVFDLGGGTFDVSVLELFEGVIEVHASAGDNFLGGEDFTHALADYFLKKH 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 271 KKKTGKDVRKDNravQKLRREVEKAKRALSSQHQAriEIESFYEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDSD 350
Cdd:cd10235 213 RLDFTSLSPSEL---AALRKRAEQAKRQLSSQDSA--EIRLTYRGEELEIELTREEFEELCAPLLERLRQPIERALRDAG 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1953100093 351 LKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAG 403
Cdd:cd10235 288 LKPSDIDAVILVGGATRMPLVRQLIARLF-GRLPLSSLDPDEAVALGAAIQAA 339
|
|
| ASKHA_NBD_HSP70_HSP105-110-like |
cd11732 |
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ... |
31-402 |
1.46e-128 |
|
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa heat shock proteins family includes the human proteins, HSPA4 (also known as 70-kDa heat shock protein 4; APG-2; HS24/P52; hsp70 RY; HSPH2), HSPA4L (also known as 70-kDa heat shock protein 4-like; APG-1; HSPH3; OSP94), and HSPH1 (also known as heat shock 105kDa/110kDa protein 1; HSP105; HSP105A; HSP105B; NY-CO-25), Saccharomyces cerevisiae Sse1p, Sse2p and a sea urchin sperm receptor. They all belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466838 [Multi-domain] Cd Length: 377 Bit Score: 384.22 E-value: 1.46e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 31 VGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEgERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQ 110
Cdd:cd11732 1 VGIDFGNQNSVVAAARRGGIDIVLNEVSNRKTPTLVGFTEK-ERLIGEAAKSQQKSNYKNTIRNFKRLIGLKFDDPEVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 111 DIKFLPFKVVE-KKTKPYIQVDIGGGQTkTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGT 189
Cdd:cd11732 80 EIKLLPFKLVElEDGKVGIEVSYNGEEV-VFSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 190 IAGLNVMRIINEPTAAAIAYGLDKR-----EGEKNILVF-DLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVM 263
Cdd:cd11732 159 IAGLNCLRLINETTAAALDYGIYKSdllesEEKPRIVAFvDMGHSSTQVSIAAFTKGKLKVLSTAFDRNLGGRDFDRALV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 264 EHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGEDFSETLTRAKFEELNMDLFRSTMKPVQ 343
Cdd:cd11732 239 EHFAEEFKKKYKIDPLENPKARLRLLDACEKLKKVLSANGEAPLNVECLMEDIDFSGQIKREEFEELIQPLLARLEAPIK 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1953100093 344 KVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQA 402
Cdd:cd11732 319 KALAQAGLTKEDLHSVEIVGGGTRVPAVKEAIAEVF-GKDLSTTLNADEAVARGCALQA 376
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
31-402 |
1.63e-126 |
|
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; This subgroup includes the human proteins, HSPA4 (also known as 70-kDa heat shock protein 4; APG-2; HS24/P52; hsp70 RY; HSPH2), HSPA4L (also known as 70-kDa heat shock protein 4-like; APG-1; HSPH3; OSP94), and HSPH1 (also known as heat shock 105kDa/110kDa protein 1; HSP105; HSP105A; HSP105B; NY-CO-25). They belong to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family, and includes proteins believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.
Pssm-ID: 466826 [Multi-domain] Cd Length: 378 Bit Score: 378.93 E-value: 1.63e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 31 VGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEgERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQ 110
Cdd:cd10228 1 VGFDFGNLSCYIAVARAGGIETIANEYSDRCTPSVVSFGEK-NRSMGVAAKNQAITNLKNTVSGFKRLLGRKFDDPFVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 111 DIKFLPFKVVEKKT-KPYIQVDIGGgQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGT 189
Cdd:cd10228 80 ELKHLPYKVVKLPNgSVGIKVQYLG-EEHVFTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 190 IAGLNVMRIINEPTAAAIAYGLDKR----EGEK--NILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVM 263
Cdd:cd10228 159 IAGLNCLRLLNDTTAVALAYGIYKQdlpaEEEKprNVVFVDMGHSSLQVSVCAFNKGKLKVLATAADPNLGGRDFDELLV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 264 EHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSS-QHQARIEIESFYEGEDFSETLTRAKFEELNMDLFRSTMKPV 342
Cdd:cd10228 239 EHFAEEFKTKYKIDVKSKPRALLRLLTECEKLKKLMSAnATELPLNIECFMDDKDVSGKMKRAEFEELCAPLFARVEVPL 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 343 QKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQA 402
Cdd:cd10228 319 RSALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKVF-GKEPSTTLNQDEAVARGCALQC 377
|
|
| ASKHA_NBD_HSP70_AtHsp70-14-like |
cd24095 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ... |
30-406 |
1.85e-118 |
|
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and similar proteins; The subgroup includes Arabidopsis thaliana Hsp70-14, also known as heat shock 70 kDa protein 14; heat shock protein 91), Hsp70-15 (also known as heat shock 70 kDa protein 15), and Hsp70-16 (also known as heat shock 70 kDa protein 16). In cooperation with other chaperones, they are key components that facilitate folding of de novo synthesized proteins, assist translocation of precursor proteins into organelles, and are responsible for degradation of damaged protein under stress conditions. Members in this subgroup belong to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family, and includes proteins believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.
Pssm-ID: 466945 [Multi-domain] Cd Length: 389 Bit Score: 358.55 E-value: 1.85e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 30 VVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTpEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQ 109
Cdd:cd24095 3 VVGIDFGNENCVVAVARKGGIDVVLNEESNRETPSMVSFG-EKQRFLGEAAAASILMNPKNTISQLKRLIGRKFDDPEVQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 110 QDIKFLPFKVVEKKT-KPYIQVDIGGGQtKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAG 188
Cdd:cd24095 82 RDLKLFPFKVTEGPDgEIGINVNYLGEQ-KVFTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLDAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 189 TIAGLNVMRIINEPTAAAIAYGL---DKREGE-KNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVME 264
Cdd:cd24095 161 QIAGLNCLRLMNETTATALAYGIyktDLPETDpTNVVFVDVGHSSTQVCVVAFKKGQLKVLSHAFDRNLGGRDFDEVLFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 265 HFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGEDFSETLTRAKFEELNMDLFRSTMKPVQK 344
Cdd:cd24095 241 HFAAEFKEKYKIDVKSNKKASLRLRAACEKVKKILSANPEAPLNIECLMEDKDVKGMITREEFEELAAPLLERLLEPLEK 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953100093 345 VLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVLS 406
Cdd:cd24095 321 ALADSGLTVDQIHSVEVVGSGSRIPAILKILTKFF-GKEPSRTMNASECVARGCALQCAMLS 381
|
|
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
29-402 |
2.03e-109 |
|
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; This subgroup includes human HYOU1 (also known as human hypoxia up-regulated 1, 170 kDa glucose-regulated protein/GRP170; HSP12A; 150 kDa oxygen-regulated protein/ORP150; GRP-170; ORP-150) and Saccharomyces cerevisiae Lhs1p (also known as Cer1p, SsI1). Mammalian HYOU1 has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. It may play a role as a molecular chaperone and participate in protein folding. HYOU1 functions as a nucleotide exchange factor (NEF) for HSPA5 (also known as BiP, Grp78 or HspA5) and may also act as a HSPA5-independent chaperone. S. cerevisiae Lhs1p, does not have a detectable endogenous ATPase activity like canonical HSP70s, but functions as a NEF for Kar2p; it's interaction with Kar2p is stimulated by nucleotide-binding. In addition, Lhs1p has a nucleotide-independent holdase activity that prevents heat-induced aggregation of proteins in vitro. Members in this subgroup belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466828 [Multi-domain] Cd Length: 353 Bit Score: 334.08 E-value: 2.03e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 29 TVVGIDLGTTYSCVGVFKNGR-VEIIANDQGNRITPSYVAFTpEGERLIGDAAKNQLTSNPENTVFDAKRLIGrtwndps 107
Cdd:cd10230 1 AVLGIDLGSEFIKVALVKPGVpFEIVLNEESKRKTPSAVAFR-NGERLFGDDALALATRFPENTFSYLKDLLG------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 108 vqqdikflpfkvvekktkpyiqvdigggqtktFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDA 187
Cdd:cd10230 73 --------------------------------YSVEELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 188 GTIAGLNVMRIINEPTAAAIAYGLDKR---EGEKNILVFDLGGGTFDVSLLTID------------NGVFEVVATNGDTH 252
Cdd:cd10230 121 AEIAGLNVLSLINDNTAAALNYGIDRRfenNEPQNVLFYDMGASSTSATVVEFSsvkekdkgknktVPQVEVLGVGWDRT 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 253 LGGEDFDQRVMEHFIKLY--KKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGEDFSETLTRAKFEEL 330
Cdd:cd10230 201 LGGLEFDLRLADHLADEFneKHKKDKDVRTNPRAMAKLLKEANRVKEVLSANTEAPASIESLYDDIDFRTKITREEFEEL 280
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953100093 331 NMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQA 402
Cdd:cd10230 281 CADLFERVVAPIEEALEKAGLTLDDIDSVELIGGGTRVPKVQEALKEALGRKELGKHLNADEAAALGAAFYA 352
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
31-406 |
1.27e-105 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and similar proteins; The subgroup includes two Saccharomyces cerevisiae heat shock protein homologs, Sse1 and Sse2. They may have calcium-dependent calmodulin-binding activities. Both Sse1 and Sse2 belong to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family, and includes proteins believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.
Pssm-ID: 466944 [Multi-domain] Cd Length: 385 Bit Score: 325.48 E-value: 1.27e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 31 VGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEgERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQ 110
Cdd:cd24094 1 VGLDLGNLNSVIAVARNRGIDIIVNEVSNRSTPSLVGFGPK-SRYLGEAAKTQETSNFKNTVGSLKRLIGRTFSDPEVAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 111 DIKFLPFKVVEKKTKPYIQVDIGGGQTKtFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTI 190
Cdd:cd24094 80 EEKYFTAKLVDANGEVGAEVNYLGEKHV-FSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 191 AGLNVMRIINEPTAAAIAYGLDK------REGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVME 264
Cdd:cd24094 159 AGLNPLRLMNDTTAAALGYGITKtdlpepEEKPRIVAFVDIGHSSYTVSIVAFKKGQLTVKGTAYDRHFGGRDFDKALTD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 265 HFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGEDFSETLTRAKFEELNMDLFRSTMKPVQK 344
Cdd:cd24094 239 HFADEFKEKYKIDVRSNPKAYFRLLAAAEKLKKVLSANAQAPLNVESLMNDIDVSSMLKREEFEELIAPLLERVTAPLEK 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953100093 345 VLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVLS 406
Cdd:cd24094 319 ALAQAGLTKDEIDFVELVGGTTRVPALKESISAFF-GKPLSTTLNQDEAVARGAAFACAILS 379
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
19-634 |
3.98e-105 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 331.05 E-value: 3.98e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 19 EEEDKKEDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGerlIGDAAKNQLTSnpentvfdAKRL 98
Cdd:PRK01433 10 EQADFKQERQIAVGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTSNN---FTIGNNKGLRS--------IKRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 99 IGRT----WNDPSVQQDIK-FLPFKVVEKKTKpyiqvdiggGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVP 173
Cdd:PRK01433 79 FGKTlkeiLNTPALFSLVKdYLDVNSSELKLN---------FANKQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 174 AYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKreGEKNI-LVFDLGGGTFDVSLLTIDNGVFEVVATNGDTH 252
Cdd:PRK01433 150 AHFNDAARGEVMLAAKIAGFEVLRLIAEPTAAAYAYGLNK--NQKGCyLVYDLGGGTFDVSILNIQEGIFQVIATNGDNM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 253 LGGEDFDQRVMEHFIKLYkkktgkDVRKDNRAVQKLRreveKAKRALSSQhqarieieSFYEGEDFSetLTRAKFEELNM 332
Cdd:PRK01433 228 LGGNDIDVVITQYLCNKF------DLPNSIDTLQLAK----KAKETLTYK--------DSFNNDNIS--INKQTLEQLIL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 333 DLFRSTMKPVQKVLEDSdlKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSrGINPDEAVAYGAAVQAGVLSGDQDtg 412
Cdd:PRK01433 288 PLVERTINIAQECLEQA--GNPNIDGVILVGGATRIPLIKDELYKAFKVDILS-DIDPDKAVVWGAALQAENLIAPHT-- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 413 DLVLLDVCPLTLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPR 492
Cdd:PRK01433 363 NSLLIDVVPLSLGMELYGGIVEKIIMRNTPIPISVVKEFTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKA 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 493 GVPQIEVTFEIDVNGILRVTAEDKGTGNKNKITITNDQNrLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSL 572
Cdd:PRK01433 443 GSIRAEVTFAIDADGILSVSAYEKISNTSHAIEVKPNHG-IDKTEIDIMLENAYKNAKIDYTTRLLQEAVIEAEALIFNI 521
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953100093 573 KNQIGDKEklggKLSSEDKETMEKAVEEKIEWLESHQDA-----DIEDFKAK-KKELEEIVQPIISKL 634
Cdd:PRK01433 522 ERAIAELT----TLLSESEISIINSLLDNIKEAVHARDIilinnSIKEFKSKiKKSMDTKLNIIINDL 585
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
29-405 |
9.55e-100 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex subunit Ssz1 and similar proteins; Ssz1, also called DnaK-related protein Ssz1, heat shock protein 70 homolog Ssz1, or pleiotropic drug resistance protein 13 (PDR13), is a component of the ribosome-associated complex (RAC), a heterodimeric chaperone complex involved in regulation of accurate translation termination and in folding or maintaining nascent polypeptides in a folding-competent state. RAC stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones Ssb1/Ssb2 that bind to the nascent polypeptide chain. Ssz1 is required for Zuo1 to function efficiently as a J-protein for Ssb1/Ssb2. It is also involved in pleiotropic drug resistance by post-translational activation of transcription factor PDR1. Members in this subfamily belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis.
Pssm-ID: 466830 [Multi-domain] Cd Length: 349 Bit Score: 308.91 E-value: 9.55e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 29 TVVGIDLGTTYSCVG-VFKNGRVEIIANDQGNRITPSYVAFTpEGERLIGDAAKNQLTSNPENTVFDAKRLIGrtwndps 107
Cdd:cd10232 1 VVIGISFGNSNSSIAiINKDGRAEVIANEDGDRQIPSILAYH-GDEEYHGSQAKAQLVRNPKNTVANFRDLLG------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 108 vqqdikflpfkvvekktkpyiqvdigggqTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDA 187
Cdd:cd10232 73 -----------------------------TTTLTVSEVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 188 GTIAGLNVMRIINEPTAAAIAYGLDKREG-----EKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRV 262
Cdd:cd10232 124 AAAAGLEVLQLIPEPAAAALAYDLRAETSgdtikDKTVVVADLGGTRSDVTVVAVRGGLYTILATVHDYELGGVALDDVL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 263 MEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGEDFSETLTRAKFEELNMDLFRSTMKPV 342
Cdd:cd10232 204 VGHFAKEFKKKTKTDPRKNARSLAKLRNAAEITKRALSQGTSAPCSVESLADGIDFHSSINRTRYELLASKVFQQFADLV 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953100093 343 QKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRG---INPDEAVAYGAAVQAGVL 405
Cdd:cd10232 284 TDAIEKAGLDPLDIDEVLLAGGASRTPKLASNFEYLFPESTIIRAptqINPDELIARGAALQASLI 349
|
|
| ASKHA_NBD_HSP70_HSPA4 |
cd11737 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ... |
29-404 |
1.00e-95 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; HSPA4, also called HSP70RY, , HS24/P52, hsp70 RY, and HSPH2, or heat shock 70-related protein APG-2, responds to acidic pH stress, is involved in the radioadaptive response, is required for normal spermatogenesis and is overexpressed in hepatocellular carcinoma. It participates in a pathway along with NBS1 (Nijmegen breakage syndrome 1, also known as p85 or nibrin), heat shock transcription factor 4b (HDF4b), and HSPA14 (belonging to a different HSP70 subfamily) that induces tumor migration, invasion, and transformation. HSPA4 expression in sperm was increased in men with oligozoospermia, especially in those with varicocele. HSPA4 belongs to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family. HSP105/110s are believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.
Pssm-ID: 466843 [Multi-domain] Cd Length: 381 Bit Score: 299.55 E-value: 1.00e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 29 TVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEgERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSV 108
Cdd:cd11737 1 SVVGFDLGFQSCYVAVARAGGIETVANEYSDRSTPACVSFGPK-NRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 109 QQDIKFLPFKVVEKKTKP------YIQvdigggQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQ 182
Cdd:cd11737 80 QAEKPSLAYELVQLPTGTtgikvmYME------EERNFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 183 ATKDAGTIAGLNVMRIINEPTAAAIAYGLDKR------EGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGE 256
Cdd:cd11737 154 SVMDATQIAGLNCLRLMNETTAVALAYGIYKQdlpapeEKPRNVVFVDMGHSAYQVSVCAFNKGKLKVLATAFDPTLGGR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 257 DFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQ-HQARIEIESFYEGEDFSETLTRAKFEELNMDLF 335
Cdd:cd11737 234 KFDEVLVNHFCEEFGKKYKLDIKSKIRALLRLFQECEKLKKLMSANaSDLPLNIECFMNDIDVSGTMNRGQFEEMCADLL 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953100093 336 RSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGV 404
Cdd:cd11737 314 ARVEPPLRSVLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFF-GKEVSTTLNADEAVARGCALQCAI 381
|
|
| ASKHA_NBD_HSP70_HSPH1 |
cd11739 |
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ... |
29-401 |
8.48e-90 |
|
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar proteins; HSPH1, also called heat shock protein 105 kDa, antigen NY-CO-25, heat shock 110 kDa protein, acts as a nucleotide-exchange factor (NEF) for chaperone proteins HSPA1A and HSPA1B, promoting the release of ADP from HSPA1A/B thereby triggering client/substrate protein release. It prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. It inhibits HSPA8/HSC70 ATPase and chaperone activities. HSPH1 belongs to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family. HSP105/110s are believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.
Pssm-ID: 466845 [Multi-domain] Cd Length: 380 Bit Score: 284.06 E-value: 8.48e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 29 TVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEgERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSV 108
Cdd:cd11739 1 SVVGFDVGFQNCYIAVARAGGIETVANEFSDRCTPSVVSFGSK-NRTIGVAAKNQQITNANNTVSNFKRFHGRAFNDPFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 109 QQDIKFLPFKVVE-KKTKPYIQVdIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDA 187
Cdd:cd11739 80 QKEKENLSYDLVPlKNGGVGVKV-MYLDEEHHFSIEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 188 GTIAGLNVMRIINEPTAAAIAYGLDKR-----EGEKNILVF-DLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQR 261
Cdd:cd11739 159 AQIVGLNCLRLMNDMTAVALNYGIYKQdlpapDEKPRIVVFvDMGHSAFQVSACAFNKGKLKVLGTAFDPYLGGRNFDEK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 262 VMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQH-QARIEIESFYEGEDFSETLTRAKFEELNMDLFRSTMK 340
Cdd:cd11739 239 LVEHFCAEFKTKYKLDVKSKIRALLRLYQECEKLKKLMSSNStDLPLNIECFMNDKDVSGKMNRSQFEELCADLLQRIEV 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953100093 341 PVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQ 401
Cdd:cd11739 319 PLYSLMEQTQLKVEDISAVEIVGGATRIPAVKERIAKFF-GKDVSTTLNADEAVARGCALQ 378
|
|
| ASKHA_NBD_HSP70_HSPA4L |
cd11738 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ... |
29-406 |
3.14e-87 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; HSPA4L, also called heat shock 70-related protein APG-1, heat-shock protein family A member 4-like protein, HSPA4-like protein, osmotic stress protein 94, or HSPH3, possesses chaperone activity in vitro where it inhibits aggregation of citrate synthase. It is expressed ubiquitously and predominantly in the testis. It is required for normal spermatogenesis and plays a role in osmotolerance. HSPA4L belongs to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family. HSP105/110s are believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.
Pssm-ID: 466844 [Multi-domain] Cd Length: 383 Bit Score: 277.57 E-value: 3.14e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 29 TVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEgERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSV 108
Cdd:cd11738 1 SVVGIDVGFQNCYIAVARSGGIETIANEYSDRCTPACVSLGSR-NRAIGNAAKSQIVTNAKNTIHGFKKFHGRAFDDPFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 109 QQDIKFLPFKVvEKKTKPYIQVDIGG-GQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDA 187
Cdd:cd11738 80 QAEKIKLPYEL-QKMPNGSTGVKVRYlDEERVFAIEQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 188 GTIAGLNVMRIINEPTAAAIAYGLDKR------EGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQR 261
Cdd:cd11738 159 AQIAGLNCLRLMNETTAVALAYGIYKQdlpaleEKPRNVVFVDMGHSAYQVSICAFNKGKLKVLATTFDPYLGGRNFDEV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 262 VMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQ-HQARIEIESFYEGEDFSETLTRAKFEELNMDLFRSTMK 340
Cdd:cd11738 239 LVDYFCEEFKTKYKLNVKENIRALLRLYQECEKLKKLMSANaSDLPLNIECFMNDIDVSSKMNRAQFEELCASLLARVEP 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953100093 341 PVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAVQAGVLS 406
Cdd:cd11738 319 PLKAVMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFF-GKDISTTLNADEAVARGCALQCAILS 383
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
31-400 |
7.38e-61 |
|
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family chaperones assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Some HSP70 family members are not chaperones but instead, function as NEFs to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle, some may function as both chaperones and NEFs. The HSP70 family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466811 [Multi-domain] Cd Length: 329 Bit Score: 206.19 E-value: 7.38e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 31 VGIDLGTTYSCVgvfkngrveiiandqgnritpSYVAFTPEGERLIGDAAKNQLTSNPENTVfdakrligrtwndPSVqq 110
Cdd:cd10170 1 VGIDFGTTYSGV---------------------AYALLGPGEPPLVVLQLPWPGGDGGSSKV-------------PSV-- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 111 dikflpfkvvekktkpyIQVdigggqtktfapeeiSAMVLTKMKETAEAYLGKKV-------THAVVTVPAYFNDAQRQA 183
Cdd:cd10170 45 -----------------LEV---------------VADFLRALLEHAKAELGDRIwelekapIEVVITVPAGWSDAAREA 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 184 TKDAGTIAGL----NVMRIINEPTAAAIAYGLDKR-----EGEKNILVFDLGGGTFDVSLLTIDNG---VFEVVATNGDT 251
Cdd:cd10170 93 LREAARAAGFgsdsDNVRLVSEPEAAALYALEDKGdllplKPGDVVLVCDAGGGTVDLSLYEVTSGsplLLEEVAPGGGA 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 252 HLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEG---EDFSETLTRAKFE 328
Cdd:cd10170 173 LLGGTDIDEAFEKLLREKLGDKGKDLGRSDADALAKLLREFEEAKKRFSGGEEDERLVPSLLGGglpELGLEKGTLLLTE 252
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953100093 329 ELNMDLFRSTMKPVQKVLED--SDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEP---SRGINPDEAVAYGAAV 400
Cdd:cd10170 253 EEIRDLFDPVIDKILELIEEqlEAKSGTPPDAVVLVGGFSRSPYLRERLRERFGSAGIiivLRSDDPDTAVARGAAL 329
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
31-400 |
1.10e-42 |
|
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar proteins; The family includes a group of uncharacterized proteins similar to Escherichia coli chaperone protein YegD that belongs to the heat shock protein 70 family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. YegD lacks the SBD. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Some family members are not chaperones but instead, function as NEFs for their Hsp70 partners, other family members function as both chaperones and NEFs.
Pssm-ID: 466829 [Multi-domain] Cd Length: 409 Bit Score: 158.98 E-value: 1.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 31 VGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERL-----IGDAAKNQLTSNPENTvfdakRLIgrtwnd 105
Cdd:cd10231 1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYFPRREEEGaesiyFGNDAIDAYLNDPEEG-----RLI------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 106 psvqQDIK-FLPFKVVEKKTKPyiqvdigggqTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQAT 184
Cdd:cd10231 70 ----KSVKsFLGSSLFDETTIF----------GRRYPFEDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFSGVGAEDD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 185 -------KDAGTIAGLNVMRIINEPTAAAIAYGLDKREgEKNILVFDLGGGTFDVSLLTID----NGVFEVVATNGDtHL 253
Cdd:cd10231 136 aqaesrlRDAARRAGFRNVEFQYEPIAAALDYEQRLDR-EELVLVVDFGGGTSDFSVLRLGpnrtDRRADILATSGV-GI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 254 GGEDFDQRVM----------------------------------EHFIKLYKKKTGKDVRKDNRAVQK------------ 287
Cdd:cd10231 214 GGDDFDRELAlkkvmphlgrgstyvsgdkglpvpawlyadlsnwHAISLLYTKKTLRLLLDLRRDAADpekierllslve 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 288 ------LRREVEKAKRALSSQHQARIEIEsfYEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIVL 361
Cdd:cd10231 294 dqlghrLFRAVEQAKIALSSADEATLSFD--FIEISIKVTITRDEFETAIAFPLARILEALERTLNDAGVKPSDVDRVFL 371
|
410 420 430
....*....|....*....|....*....|....*....
gi 1953100093 362 VGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGAAV 400
Cdd:cd10231 372 TGGSSQSPAVRQALASLF-GQARLVEGDEFGSVAAGLAL 409
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
30-399 |
4.60e-24 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar proteins; The family includes heat shock 70 kDa proteins HSPA12A and HSPA12B. HSPA12A is an adapter protein for SORL1, but not SORT1. It delays SORL1 internalization and affects SORL1 subcellular localization. HSPA12B, predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. It may be important for host defense in microglia-mediated immune response. Both HSPA12A and HSPA12B belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12A and HSPA12B.
Pssm-ID: 466827 [Multi-domain] Cd Length: 372 Bit Score: 104.28 E-value: 4.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 30 VVGIDLGTTYSCVG---VFKNGRVEIIANDQG------NRITPSYVAFTPEGERL-IGDAAKNQLTSNPENtvfDAKRLI 99
Cdd:cd10229 2 VVAIDFGTTYSGYAysfITDPGDIHTMYNWWGaptgvsSPKTPTCLLLNPDGEFHsFGYEAREKYSDLAED---EEHQWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 100 GRtwndpsvQQDIKFLPFKvvEKKTKPYIQVDIGGgqtKTFAPEEISAMVLTKMKETAEAYLGKKVTHA--------VVT 171
Cdd:cd10229 79 YF-------FKFKMMLLSE--KELTRDTKVKAVNG---KSMPALEVFAEALRYLKDHALKELRDRSGSSldeddirwVLT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 172 VPAYFNDAQ----RQATKDAGTIAGLNVMR--IINEPTAAAIAYGLDKREGEKNI-------LVFDLGGGTFDVSLLTI- 237
Cdd:cd10229 147 VPAIWSDAAkqfmREAAVKAGLISEENSEQliIALEPEAAALYCQKLLAEGEEKElkpgdkyLVVDCGGGTVDITVHEVl 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 238 -DNGVFEVVATNGDtHLGGEDFDQRvmehFIKLYKKKTGKDVRKDNR-----AVQKLRREVEKAKRAlssqhqarieies 311
Cdd:cd10229 227 eDGKLEELLKASGG-PWGSTSVDEE----FEELLEEIFGDDFMEAFKqkypsDYLDLLQAFERKKRS------------- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 312 fyegedFSETLTRAKFEELNMDLFRSTMKPVQKVLEDSDLKksDIDEIVLVGGSTRIPKIQQLVKEFFngkEPSRGI--- 388
Cdd:cd10229 289 ------FKLRLSPELMKSLFDPVVKKIIEHIKELLEKPELK--GVDYIFLVGGFAESPYLQKAVKEAF---STKVKIiip 357
|
410
....*....|..
gi 1953100093 389 -NPDEAVAYGAA 399
Cdd:cd10229 358 pEPGLAVVKGAV 369
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
31-400 |
7.69e-13 |
|
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and similar proteins; MreB proteins are bacterial actin homologs that may play a role in cell shape determination by positioning the cell wall synthetic machinery. MreB has also been implicated in chromosome segregation; specifically, MreB is thought to bind to and segregate the replication origin of bacterial chromosomes. The family includes three MreB isoforms, MreB (also called actin-like MreB protein or rod shape-determining protein MreB), Mbl (also called actin-like Mbl protein or rod shape-determining protein Mbl) and MreBH (also called actin-like MreBH protein or rod shape-determining protein MreBH), in cell morphogenesis of Bacillus subtilis. All isoforms can support rod-shaped cell growth normal conditions. They form membrane-associated dynamic filaments that are essential for cell shape determination. They act by regulating cell wall synthesis and cell elongation, and thus cell shape. The feedback loops between cell geometry and their localizations may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature. Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on their polymerization. They organize peptidoglycan synthesis in the lateral cell wall. MreB, Mbl and MreBH can form a complex. The MreB-like family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466824 [Multi-domain] Cd Length: 317 Bit Score: 69.81 E-value: 7.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 31 VGIDLGTTYSCVGVFKNGrveIIANDqgnritPSYVAFTPEGERLI--GDaaknqltsnpentvfDAKRLIGRTwndpsv 108
Cdd:cd10225 2 IGIDLGTANTLVYVKGKG---IVLNE------PSVVAVDKNTGKVLavGE---------------EAKKMLGRT------ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 109 qqdikflpfkvvekktkpyiqvdigggqtktfaPEEISAM------VLTKMkETAEAYLG---KKV--------THAVVT 171
Cdd:cd10225 52 ---------------------------------PGNIVAIrplrdgVIADF-EATEAMLRyfiRKAhrrrgflrPRVVIG 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 172 VPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNiLVFDLGGGTFDVSLLTIdNGvfeVVATNGdT 251
Cdd:cd10225 98 VPSGITEVERRAVKEAAEHAGAREVYLIEEPMAAAIGAGLPIEEPRGS-MVVDIGGGTTEIAVISL-GG---IVTSRS-V 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 252 HLGGEDFDQRVMEHFIKLYKKKTGkdvrkdnravqklRREVEKAKRALSSQHQARIEIESFYEGEDF------SETLTRA 325
Cdd:cd10225 172 RVAGDEMDEAIINYVRRKYNLLIG-------------ERTAERIKIEIGSAYPLDEELSMEVRGRDLvtglprTIEITSE 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 326 KFEELNMDLFRSTMKPVQKVLEDS--DLkKSDIDE--IVLVGGSTRIPKIQQLVKEFFngkepsrGI------NPDEAVA 395
Cdd:cd10225 239 EVREALEEPVNAIVEAVRSTLERTppEL-AADIVDrgIVLTGGGALLRGLDELLREET-------GLpvhvadDPLTCVA 310
|
....*
gi 1953100093 396 YGAAV 400
Cdd:cd10225 311 KGAGK 315
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
147-374 |
6.58e-12 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 67.96 E-value: 6.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 147 AMVLtKMKETAEAYLGKKVTHAVVTVPAYFN-----DAQRQAT---KDAGTIAGLNVMRIINEPTAAAIAY--GLDKreg 216
Cdd:PRK11678 132 AMML-HIKQQAEAQLQAAITQAVIGRPVNFQglggeEANRQAEgilERAAKRAGFKDVEFQFEPVAAGLDFeaTLTE--- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 217 EKNILVFDLGGGTFDVSLLT-----IDNgvfevvaTNGDTHL--------GGEDFD-QRVMEHFIKLY----KKKTGK-- 276
Cdd:PRK11678 208 EKRVLVVDIGGGTTDCSMLLmgpswRGR-------ADRSASLlghsgqriGGNDLDiALAFKQLMPLLgmgsETEKGIal 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 277 ------------------------------DVRKDNRAVQKLRR---------------EVEKAKRALSSQHQARIEIeS 311
Cdd:PRK11678 281 pslpfwnavaindvpaqsdfyslangrllnDLIRDAREPEKVARllkvwrqrlsyrlvrSAEEAKIALSDQAETRASL-D 359
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953100093 312 FYEgEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDSDLKKsdiDEIVLVGGSTRIP----KIQQL 374
Cdd:PRK11678 360 FIS-DGLATEISQQGLEEAISQPLARILELVQLALDQAQVKP---DVIYLTGGSARSPliraALAQQ 422
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
31-399 |
2.07e-09 |
|
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];
Pssm-ID: 440695 [Multi-domain] Cd Length: 339 Bit Score: 59.71 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 31 VGIDLGTTYSCVGVFKNGrveIIANDqgnritPSYVAFTPEGERLI--GDaaknqltsnpentvfDAKRLIGRTwndpsv 108
Cdd:COG1077 10 IGIDLGTANTLVYVKGKG---IVLNE------PSVVAIDKKTGKVLavGE---------------EAKEMLGRT------ 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 109 qqdikflpfkvvekktkpyiqvdigggqtktfaPEEISAMvlTKMK-------ETAEAYLG---KKVT--------HAVV 170
Cdd:COG1077 60 ---------------------------------PGNIVAI--RPLKdgviadfEVTEAMLKyfiKKVHgrrsffrpRVVI 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 171 TVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVfDLGGGTFDVSLltIDNGvfEVVATNGd 250
Cdd:COG1077 105 CVPSGITEVERRAVRDAAEQAGAREVYLIEEPMAAAIGAGLPIEEPTGNMVV-DIGGGTTEVAV--ISLG--GIVVSRS- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 251 THLGGEDFDQRVMEHFIKLYKKKTGkdvrkdnravqklRREVEKAKRALSSQHQARIEIESFYEGEDFSETLTRAKfeEL 330
Cdd:COG1077 179 IRVAGDELDEAIIQYVRKKYNLLIG-------------ERTAEEIKIEIGSAYPLEEELTMEVRGRDLVTGLPKTI--TI 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 331 NMDLFRSTMKP--------VQKVLEDS--DLkKSDIDE--IVLVGGSTRIPKIQQLVKEFFngkepsrGI------NPDE 392
Cdd:COG1077 244 TSEEIREALEEplnaiveaIKSVLEKTppEL-AADIVDrgIVLTGGGALLRGLDKLLSEET-------GLpvhvaeDPLT 315
|
....*..
gi 1953100093 393 AVAYGAA 399
Cdd:COG1077 316 CVARGTG 322
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
119-380 |
6.70e-09 |
|
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes type IV pilus inner membrane component PilM, cell division protein FtsA, and ethanolamine utilization protein EutJ. PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity. Members in PilM-like family belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466854 [Multi-domain] Cd Length: 282 Bit Score: 57.30 E-value: 6.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 119 VVEKKTKPYIQVDIGGGQTKTFA--------PEEIsAMVLTKMKETAEAYLGKKVTHAVVTVP----AYFNDAQRqatkd 186
Cdd:cd24004 14 VLEEDDENIEVLAFSSEEHPERAmgdgqihdISKV-AESIKELLKELEEKLGSKLKDVVIAIAkvveSLLNVLEK----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 187 agtiAGLNVMRIINEPTAAAIAYGLDKrEGEKNILVFDLGGGTFDVSLltIDNGVfeVVATnGDTHLGGEDFDQRVMEHF 266
Cdd:cd24004 88 ----AGLEPVGLTLEPFAAANLLIPYD-MRDLNIALVDIGAGTTDIAL--IRNGG--IEAY-RMVPLGGDDFTKAIAEGF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 267 IKLYKkktgkdvrkdnravqklrrEVEKAKRALSSQhqarieiESFYEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVL 346
Cdd:cd24004 158 LISFE-------------------EAEKIKRTYGIF-------LLIEAKDQLGFTINKKEVYDIIKPVLEELASGIANAI 211
|
250 260 270
....*....|....*....|....*....|....
gi 1953100093 347 EDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFN 380
Cdd:cd24004 212 EEYNGKFKLPDAVYLVGGGSKLPGLNEALAEKLG 245
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
149-253 |
5.01e-08 |
|
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity.
Pssm-ID: 466897 [Multi-domain] Cd Length: 241 Bit Score: 54.19 E-value: 5.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 149 VLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLdkregeKNILVFDLGGG 228
Cdd:cd24047 48 IVRKLKETLEKKLGVELTSAATAFPPGTGERDARAIRNVLEGAGLEVSNVVDEPTAANAVLGI------RDGAVVDIGGG 121
|
90 100
....*....|....*....|....*....
gi 1953100093 229 TFDVSLltIDNGvfEVVAT----NGDTHL 253
Cdd:cd24047 122 TTGIAV--LKDG--KVVYTadepTGGTHL 146
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
167-399 |
2.33e-07 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 53.21 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 167 HAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNiLVFDLGGGTFDVSLLTIDNgvfevVA 246
Cdd:PRK13930 102 RIVICVPSGITEVERRAVREAAEHAGAREVYLIEEPMAAAIGAGLPVTEPVGN-MVVDIGGGTTEVAVISLGG-----IV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 247 TNGDTHLGGEDFDQRVMEHFIKLYKKKTGKdvrkdnravqklrREVEKAKR----ALSSQHQARIEIesfyEGEDFSETL 322
Cdd:PRK13930 176 YSESIRVAGDEMDEAIVQYVRRKYNLLIGE-------------RTAEEIKIeigsAYPLDEEESMEV----RGRDLVTGL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 323 trAKFEELNMDLFRSTMKP--------VQKVLEDS--DLkKSDIDE--IVLVGGSTRIPKIQQLVKEFFngkepsrGI-- 388
Cdd:PRK13930 239 --PKTIEISSEEVREALAEplqqiveaVKSVLEKTppEL-AADIIDrgIVLTGGGALLRGLDKLLSEET-------GLpv 308
|
250
....*....|....*
gi 1953100093 389 ----NPDEAVAYGAA 399
Cdd:PRK13930 309 hiaeDPLTCVARGTG 323
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
28-271 |
4.55e-07 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 52.21 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 28 GTVVGIDLGTtySCVGVFKNGRvEIIANDqgnritPSYVAFtpegerligDAAKNQLTSNPEntvfDAKRLIGRTwndPS 107
Cdd:PRK13928 3 GRDIGIDLGT--ANVLVYVKGK-GIVLNE------PSVVAI---------DKNTNKVLAVGE----EARRMVGRT---PG 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 108 VQQDIKFLP------FKVVEKKTKPYIQVdiGGGQTKTFAPEeisamvltkmketaeaylgkkvthAVVTVPAYFNDAQR 181
Cdd:PRK13928 58 NIVAIRPLRdgviadYDVTEKMLKYFINK--ACGKRFFSKPR------------------------IMICIPTGITSVEK 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 182 QATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVfDLGGGTFDVSLLTIDNGVfevvaTNGDTHLGGEDFDQR 261
Cdd:PRK13928 112 RAVREAAEQAGAKKVYLIEEPLAAAIGAGLDISQPSGNMVV-DIGGGTTDIAVLSLGGIV-----TSSSIKVAGDKFDEA 185
|
250
....*....|
gi 1953100093 262 VMEHFIKLYK 271
Cdd:PRK13928 186 IIRYIRKKYK 195
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
29-270 |
2.29e-06 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 50.29 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 29 TVVGIDLGTTYSCVGVFKNGrveIIANDqgnritPSYVAFTPEGERLIGDAAknqltsnpentvfDAKRLIGRTwndpsv 108
Cdd:PRK13929 5 TEIGIDLGTANILVYSKNKG---IILNE------PSVVAVDTETKAVLAIGT-------------EAKNMIGKT------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 109 qqdikflPFKVVekKTKPYiqvdigggQTKTFAPEEISAMVLTKMKETAEAYLGKKV--THAVVTVPAYFNDAQRQATKD 186
Cdd:PRK13929 57 -------PGKIV--AVRPM--------KDGVIADYDMTTDLLKQIMKKAGKNIGMTFrkPNVVVCTPSGSTAVERRAISD 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 187 AGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVfDLGGGTFDVSLLTidngvFEVVATNGDTHLGGEDFDQRVMEHF 266
Cdd:PRK13929 120 AVKNCGAKNVHLIEEPVAAAIGADLPVDEPVANVVV-DIGGGTTEVAIIS-----FGGVVSCHSIRIGGDQLDEDIVSFV 193
|
....
gi 1953100093 267 IKLY 270
Cdd:PRK13929 194 RKKY 197
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
149-253 |
2.41e-06 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 49.44 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 149 VLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLdkregeKNILVFDLGGG 228
Cdd:PRK15080 72 IVRRLKATLEEKLGRELTHAATAIPPGTSEGDPRAIINVVESAGLEVTHVLDEPTAAAAVLGI------DNGAVVDIGGG 145
|
90 100
....*....|....*....|....*....
gi 1953100093 229 TFDVSLLtiDNGvfEVVAT----NGDTHL 253
Cdd:PRK15080 146 TTGISIL--KDG--KVVYSadepTGGTHM 170
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
31-398 |
8.63e-06 |
|
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two related archaeal sequences. MreB is known to be a rod shape-determining protein in bacteria and goes to make up the bacterial cytoskeleton. Genes coding for MreB/Mbl are only found in elongated bacteria, not in coccoid forms. It has been speculated that constituents of the eukaryotic cytoskeleton (tubulin, actin) may have evolved from prokaryotic precursor proteins closely related to today's bacterial proteins FtsZ and MreB/Mbl.
Pssm-ID: 399596 [Multi-domain] Cd Length: 327 Bit Score: 48.32 E-value: 8.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 31 VGIDLGTTYSCVGVFKNGrveIIANDqgnritPSYVAFTPEGERLI--GDaaknqltsnpentvfDAKRLIGRTwndpsv 108
Cdd:pfam06723 4 IGIDLGTANTLVYVKGKG---IVLNE------PSVVAINTKTKKVLavGN---------------EAKKMLGRT------ 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 109 qqdikflpfkvvekktkpyiqvdigggqtktfaPEEISAM------VLTKMkETAEA---YLGKKVTHA--------VVT 171
Cdd:pfam06723 54 ---------------------------------PGNIVAVrplkdgVIADF-EVTEAmlkYFIKKVHGRrsfskprvVIC 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 172 VPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNiLVFDLGGGTFDVSLLTIdNGVfeVVATNgdT 251
Cdd:pfam06723 100 VPSGITEVERRAVKEAAKNAGAREVFLIEEPMAAAIGAGLPVEEPTGN-MVVDIGGGTTEVAVISL-GGI--VTSKS--V 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 252 HLGGEDFDQRVMEHFIKLYKKKTGKdvrkdnravqklrREVEKAKRALSSQHQARIEIESFYEGEDFSETLTR------A 325
Cdd:pfam06723 174 RVAGDEFDEAIIKYIRKKYNLLIGE-------------RTAERIKIEIGSAYPTEEEEKMEIRGRDLVTGLPKtieissE 240
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953100093 326 KFEELNMDLFRSTMKPVQKVLEDS--DLkKSDIDE--IVLVGGSTRIPKIQQLVKEFFnGKEPSRGINPDEAVAYGA 398
Cdd:pfam06723 241 EVREALKEPVSAIVEAVKEVLEKTppEL-AADIVDrgIVLTGGGALLRGLDKLLSDET-GLPVHIAEDPLTCVALGT 315
|
|
| ASKHA_ATPase-like |
cd00012 |
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ... |
168-266 |
2.78e-04 |
|
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.
Pssm-ID: 466786 [Multi-domain] Cd Length: 135 Bit Score: 41.30 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 168 AVVTVPAYFNDAQRQAT-----------KDAGTIAGLNVMRIINEPTAAAIAYGLDKREGekNILVFDLGGGTfdvsllt 236
Cdd:cd00012 16 IVITVAAGDRDANRVATiteailllqtnAATFALFTGPPVRIVNEAVAAAIGALLTLGPE--GLLVVDLGGGT------- 86
|
90 100 110
....*....|....*....|....*....|
gi 1953100093 237 idNGVFEVVATNGDTHLggEDFDQRVMEHF 266
Cdd:cd00012 87 --DISANVVLVGGGARN--NGLAKRLKELL 112
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
355-407 |
5.89e-04 |
|
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466809 [Multi-domain] Cd Length: 443 Bit Score: 42.92 E-value: 5.89e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1953100093 355 DIDEIVLVGGSTRIPKIQQLVKEFFNgkEPSRGINPDEAVAYGAAVQAGVLSG 407
Cdd:cd07809 393 EIDEIRLIGGGSKSPVWRQILADVFG--VPVVVPETGEGGALGAALQAAWGAG 443
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
536-639 |
9.27e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 9.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 536 EEIERMVNDAEKFAEEDKKLK------ERIDTRNELESYAYSLKNQIGDKEK-LGGKLSSEDK--ETMEKAvEEKIEWLE 606
Cdd:PRK12704 38 EEAKRILEEAKKEAEAIKKEAlleakeEIHKLRNEFEKELRERRNELQKLEKrLLQKEENLDRklELLEKR-EEELEKKE 116
|
90 100 110
....*....|....*....|....*....|...
gi 1953100093 607 SHQDADIEDFKAKKKELEEIVQPIISKLYGSAG 639
Cdd:PRK12704 117 KELEQKQQELEKKEEELEELIEEQLQELERISG 149
|
|
| Hydantoinase_A |
pfam01968 |
Hydantoinase/oxoprolinase; This family includes the enzymes hydantoinase and oxoprolinase EC:3. ... |
145-245 |
9.36e-04 |
|
Hydantoinase/oxoprolinase; This family includes the enzymes hydantoinase and oxoprolinase EC:3.5.2.9. Both reactions involve the hydrolysis of 5-membered rings via hydrolysis of their internal imide bonds.
Pssm-ID: 396517 [Multi-domain] Cd Length: 288 Bit Score: 41.50 E-value: 9.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 145 ISAMVLTKMKETAEAyLGKKVTHAVVTVPAYFNDAQRQATkDAGTIAGLNVMRIINEPTAAAIAYG-LDKREGEKNILVF 223
Cdd:pfam01968 7 VNAYLAPIMREYLEG-VEDSLEKVGSKAPVYVMQSDGGLV-SIDEARKRPVETILSGPAAGVVGAAyTGKLLGNKNLIGF 84
|
90 100
....*....|....*....|..
gi 1953100093 224 DLGGGTFDVSLltIDNGVFEVV 245
Cdd:pfam01968 85 DMGGTSTDISP--IIDGEPEIT 104
|
|
| HyuA |
COG0145 |
N-methylhydantoinase A/oxoprolinase/acetone carboxylase, beta subunit [Amino acid transport ... |
204-255 |
1.05e-03 |
|
N-methylhydantoinase A/oxoprolinase/acetone carboxylase, beta subunit [Amino acid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 439915 [Multi-domain] Cd Length: 678 Bit Score: 42.38 E-value: 1.05e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1953100093 204 AAAIAygldKREGEKNILVFDLGGGTFDVSLltIDNGVFEVVAtngDTHLGG 255
Cdd:COG0145 266 AAALA----RAAGFDNVITFDMGGTSTDVSL--IEDGEPERTT---ETEVAG 308
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
169-265 |
1.67e-03 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 41.23 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 169 VVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVfDLGGGTFDVSLLTIdNGvfevVATN 248
Cdd:PRK13927 100 VICVPSGITEVERRAVRESALGAGAREVYLIEEPMAAAIGAGLPVTEPTGSMVV-DIGGGTTEVAVISL-GG----IVYS 173
|
90
....*....|....*..
gi 1953100093 249 GDTHLGGEDFDQRVMEH 265
Cdd:PRK13927 174 KSVRVGGDKFDEAIINY 190
|
|
| ASKHA_NBD_PilM |
cd24049 |
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ... |
191-400 |
2.43e-03 |
|
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar proteins; PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. PilN/PilO heterodimers form the foundation of the inner-membrane PilM/PilN/PilO/PilP complex which plays an essential role in the assembly of a functional T4 pilus. In turn, PilM associates with PilN and facilitates PilM functionally relevant structural changes that differentially impacts PilM binding to PilB, PilT, and PilC.
Pssm-ID: 466899 [Multi-domain] Cd Length: 339 Bit Score: 40.72 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 191 AGLNVMRIINEPTAAAIAYGLDKR-EGEKNILVFDLGGGTFDVSLltIDNGVFEVVATNGdthLGGEDFDQRVMEHFikl 269
Cdd:cd24049 148 AGLKPVAIDVESFALARALEYLLPdEEEETVALLDIGASSTTLVI--VKNGKLLFTRSIP---VGGNDITEAIAKAL--- 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 270 ykkktgkDVRKDnravqklrrEVEKAKRalssqHQARIEIESFYEGEDFSETLTRAkFEELNMDLFRStmkpvqkvLE-- 347
Cdd:cd24049 220 -------GLSFE---------EAEELKR-----EYGLLLEGEEGELKKVAEALRPV-LERLVSEIRRS--------LDyy 269
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 348 DSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGK----EPSRGINPDE-------------AVAYGAAV 400
Cdd:cd24049 270 RSQNGGEPIDKIYLTGGGSLLPGLDEYLSERLGIPveilNPFSNIESKKsddeelkedaplfAVAIGLAL 339
|
|
| ASKHA_NBD_ParM-like |
cd10227 |
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ... |
31-283 |
2.53e-03 |
|
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ParM is a plasmid-encoded bacterial homolog of actin, which polymerizes into filaments similar to F-actin, and plays a vital role in plasmid segregation. ParM filaments segregate plasmids paired at midcell into the individual daughter cells. This subfamily also contains Thermoplasma acidophilum Ta0583, an active ATPase at physiological temperatures, which has a propensity to form filaments. ParM-like proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466825 [Multi-domain] Cd Length: 263 Bit Score: 40.20 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 31 VGIDLGttyscvgvfkNGRVEIIANDQGNRITPSYVAFTPEGERLIGDaaknqlTSNPENTVFDAKR-LIGrtwndpsvq 109
Cdd:cd10227 1 IGIDIG----------NGNTKVVTGGGKEFKFPSAVAEARESSLDDGL------LEDDIIVEYNGKRyLVG--------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 110 qdikflpfKVVEKKTKPYIQVDIGGGQTKTFApeeisAMVLTKMKETAEAYlgKKVTHAVVTVPA--YFNDAQRQATKDA 187
Cdd:cd10227 56 --------ELALREGGGGRSTGDDKKKSEDAL-----LLLLAALALLGDDE--EVDVNLVVGLPIseYKEEKKELKKKLL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 188 GTIAGLNVM-----------RIINEPTAAAIAYGLDKREGE-KNILVFDLGGGTFDVslLTIDNGvfEVVATNGDTHLGG 255
Cdd:cd10227 121 KGLHEFTFNgkerritindvKVLPEGAGAYLDYLLDDDELEdGNVLVIDIGGGTTDI--LTFENG--KPIEESSDTLPGG 196
|
250 260
....*....|....*....|....*...
gi 1953100093 256 EDFDQRVMEHFIKLYKKKTGKDVRKDNR 283
Cdd:cd10227 197 EEALEKYADDILNELLKKLGDELDSADK 224
|
|
| ASKHA_NBD_PPX_GppA |
cd24006 |
nucleotide-binding domain (NBD) of the exopolyphosphatase/guanosine pentaphosphate ... |
117-330 |
8.72e-03 |
|
nucleotide-binding domain (NBD) of the exopolyphosphatase/guanosine pentaphosphate phosphohydrolase (PPX/GppA) domain family; Members of the PPX/GppA family are involved in bacterial survival and metabolism. They may play distinct biochemical roles involved in polyphosphate and (p)ppGpp metabolic pathways. Guanosine pentaphosphate (pppGpp) phosphohydrolase (GppA; EC 3.6.1.40) plays a key role in (p)ppGpp homeostasis. It specifically catalyzes the conversion of pppGpp to ppGpp (guanosine tetraphosphate). Sharing a similar domain structure, GppA is indistinguishable from exopolyphosphatase (PPX; EC 3.6.1.11), which mediates the metabolism of cellular inorganic polyphosphate. Especially, it is responsible for the maintenance of appropriate levels of cellular inorganic polyphosphate (PolyP). Some bacteria, such as Escherichia coli, possesses two homologs, EcGppA and EcPPX. Some others, such as Helicobacter pylori and Aquifex aeolicus, encode only one PPX/GppA homolog, which may play important roles in the homeostasis of both (p)ppGpp and PolyP. The PPX/GppA family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466856 [Multi-domain] Cd Length: 294 Bit Score: 38.67 E-value: 8.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 117 FKVVEKKTKPyiqVDIGGG--QTKTFAPEEISAMV--LTKMKETAEAYLGKKV----THAVvtvpayfndaqRQAtKDAG 188
Cdd:cd24006 23 FRILERLREP---VRLGEDvfTTGRISEEAIERAVeaLRRFKKLADEYGVKRIravaTSAV-----------REA-SNGD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 189 TI-------AGLNVmRIINEP-----TAAAIAYGLDKreGEKNILVFDLGGGTFDVSLLtiDNGVFEVVATngdTHLGGe 256
Cdd:cd24006 88 EFlerikreTGIDV-EIISGEeearlIYLAVRSGLPL--GDGNALIVDIGGGSTELTLG--DNGEILFSES---LPLGA- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953100093 257 dfdQRVMEHFIKLYkkktgkdvRKDNRAVQKLRREVEKAKRALSSQHQ--------------ARIEIESFYEGEDFSETL 322
Cdd:cd24006 159 ---VRLTERFLKDD--------PPSELLEEYLRSFVRSVLRPLPKRRKikfdvaigsggtilALAAMALARKGKPHGYEI 227
|
....*...
gi 1953100093 323 TRAKFEEL 330
Cdd:cd24006 228 SREELKAL 235
|
|
| |
